메뉴 건너뛰기




Volumn 8, Issue 8, 2016, Pages

Signaling receptors for TGF-β family members

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; MICRORNA; TRANSFORMING GROWTH FACTOR BETA; TRANSFORMING GROWTH FACTOR BETA RECEPTOR;

EID: 84982840895     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a022053     Document Type: Article
Times cited : (508)

References (287)
  • 2
    • 0030613249 scopus 로고    scopus 로고
    • TbRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling
    • Abdollah S, Macías-Silva M, Tsukazaki T, Hayashi H, Attisano L, Wrana JL. 1997. TbRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling. J Biol Chem 272: 27678-27685.
    • (1997) J Biol Chem , vol.272 , pp. 27678-27685
    • Abdollah, S.1    Macías-Silva, M.2    Tsukazaki, T.3    Hayashi, H.4    Attisano, L.5    Wrana, J.L.6
  • 3
    • 84866985855 scopus 로고    scopus 로고
    • Targeting the TGFb signalling pathway in disease
    • Akhurst RJ, Hata A. 2012. Targeting the TGFb signalling pathway in disease. Nat Rev Drug Discov 11: 790-811.
    • (2012) Nat Rev Drug Discov , vol.11 , pp. 790-811
    • Akhurst, R.J.1    Hata, A.2
  • 11
    • 78651102047 scopus 로고    scopus 로고
    • TbRI/Alk5-independent TbRII signaling to ERK1/2 in human skin cells according to distinct levels of TbRII expression
    • Bandyopadhyay B, Han A, Dai J, Fan J, Li Y, Chen M, Woodley DT, Li W. 2011. TbRI/Alk5-independent TbRII signaling to ERK1/2 in human skin cells according to distinct levels of TbRII expression. J Cell Sci 124: 19-24.
    • (2011) J Cell Sci , vol.124 , pp. 19-24
    • Bandyopadhyay, B.1    Han, A.2    Dai, J.3    Fan, J.4    Li, Y.5    Chen, M.6    Woodley, D.T.7    Li, W.8
  • 12
    • 0033534572 scopus 로고    scopus 로고
    • Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-b superfamily
    • Barbara NP, Wrana JL, Letarte M. 1999. Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-b superfamily. J Biol Chem 274: 584-594.
    • (1999) J Biol Chem , vol.274 , pp. 584-594
    • Barbara, N.P.1    Wrana, J.L.2    Letarte, M.3
  • 14
    • 53349156578 scopus 로고    scopus 로고
    • Two highly related regulatory subunits of PP2A exert opposite effects on TGF-β/activin/nodal signalling
    • Batut J, Schmierer B, Cao J, Raftery LA, Hill CS, Howell M. 2008. Two highly related regulatory subunits of PP2A exert opposite effects on TGF-β/activin/nodal signalling. Development 135: 2927-2937.
    • (2008) Development , vol.135 , pp. 2927-2937
    • Batut, J.1    Schmierer, B.2    Cao, J.3    Raftery, L.A.4    Hill, C.S.5    Howell, M.6
  • 16
    • 38048999928 scopus 로고    scopus 로고
    • Mutational inactivation of TGFBR2 in microsatellite unstable colon cancer arises from the cooperation of genomic instability and the clonal outgrowth of transforming growth factor b resistant cells
    • Biswas S, Trobridge P, Romero-Gallo J, Billheimer D, Myeroffs LL, Willson JKV, Markowitz SD, Grady WM. 2008. Mutational inactivation of TGFBR2 in microsatellite unstable colon cancer arises from the cooperation of genomic instability and the clonal outgrowth of transforming growth factor b resistant cells. Genes Chromos Cancer 47: 95-106.
    • (2008) Genes Chromos Cancer , vol.47 , pp. 95-106
    • Biswas, S.1    Trobridge, P.2    Romero-Gallo, J.3    Billheimer, D.4    Myeroffs, L.L.5    Willson, J.6    Markowitz, S.D.7    Grady, W.M.8
  • 18
    • 84055177056 scopus 로고    scopus 로고
    • CD109-mediated degradation of TGF-β receptors and inhibition of TGF-β responses involve regulation of SMAD7 and Smurf2 localization and function
    • Bizet AA, Tran-Khanh N, Saksena A, Liu K, Buschmann MD, Philip A. 2012. CD109-mediated degradation of TGF-β receptors and inhibition of TGF-β responses involve regulation of SMAD7 and Smurf2 localization and function. J Cell Biochem 113: 238-246.
    • (2012) J Cell Biochem , vol.113 , pp. 238-246
    • Bizet, A.A.1    Tran-Khanh, N.2    Saksena, A.3    Liu, K.4    Buschmann, M.D.5    Philip, A.6
  • 19
    • 0037131169 scopus 로고    scopus 로고
    • Hyaluronan promotes signaling interaction between CD44 and the transforming growth factor b receptor I in metastatic breast tumor cells
    • Bourguignon LY, Singleton PA, Zhu H, Zhou B. 2002. Hyaluronan promotes signaling interaction between CD44 and the transforming growth factor b receptor I in metastatic breast tumor cells. J Biol Chem 277: 39703-39712.
    • (2002) J Biol Chem , vol.277 , pp. 39703-39712
    • Bourguignon, L.Y.1    Singleton, P.A.2    Zhu, H.3    Zhou, B.4
  • 20
    • 66949118228 scopus 로고    scopus 로고
    • Interleukin-6 modulates the expression of the bone morphogenic protein receptor type II through a novel STAT3-microRNA cluster 17/92 pathway
    • Brock M, Trenkmann M, Gay RE, Michel BA, Gay S, Fischler M, Ulrich S, Speich R, Huber LC. 2009. Interleukin-6 modulates the expression of the bone morphogenic protein receptor type II through a novel STAT3-microRNA cluster 17/92 pathway. Circ Res 104: 1184-1191.
    • (2009) Circ Res , vol.104 , pp. 1184-1191
    • Brock, M.1    Trenkmann, M.2    Gay, R.E.3    Michel, B.A.4    Gay, S.5    Fischler, M.6    Ulrich, S.7    Speich, R.8    Huber, L.C.9
  • 22
    • 84942915954 scopus 로고    scopus 로고
    • The insulin response integrates increased TGF-β signaling through Akt-induced enhancement of cell surface delivery of TGF-β receptors
    • Budi EH, Muthusamy BP, Derynck R. 2015. The insulin response integrates increased TGF-β signaling through Akt-induced enhancement of cell surface delivery of TGF-β receptors. Sci Signal 8: e80630.
    • (2015) Sci Signal , vol.8
    • Budi, E.H.1    Muthusamy, B.P.2    Derynck, R.3
  • 26
    • 34547882714 scopus 로고    scopus 로고
    • A novel regulatory mechanism of the bone morphogenetic protein (BMP) signaling pathway involving the carboxyl-terminal tail domain of BMP type II receptor
    • Chan MC, Nguyen PH, Davis BN, Ohoka N, Hayashi H, Du K, Lagna G, Hata A. 2007. A novel regulatory mechanism of the bone morphogenetic protein (BMP) signaling pathway involving the carboxyl-terminal tail domain of BMP type II receptor. Mol Cell Biol 27: 5776-5789.
    • (2007) Mol Cell Biol , vol.27 , pp. 5776-5789
    • Chan, M.C.1    Nguyen, P.H.2    Davis, B.N.3    Ohoka, N.4    Hayashi, H.5    Du, K.6    Lagna, G.7    Hata, A.8
  • 27
    • 76349093390 scopus 로고    scopus 로고
    • Molecular basis for antagonism between PDGF and the TGFb family of signalling pathways by control of miR-24 expression
    • Chan MC, Hilyard AC, Wu C, Davis BN, Hill NS, Lal A, Lieberman J, Lagna G, Hata A. 2010. Molecular basis for antagonism between PDGF and the TGFb family of signalling pathways by control of miR-24 expression. EMBO J 29: 559-573.
    • (2010) EMBO J , vol.29 , pp. 559-573
    • Chan, M.C.1    Hilyard, A.C.2    Wu, C.3    Davis, B.N.4    Hill, N.S.5    Lal, A.6    Lieberman, J.7    Lagna, G.8    Hata, A.9
  • 29
    • 0028059199 scopus 로고
    • Homomeric interactions between type II transforming growth factor-b receptors
    • Chen RH, Derynck R. 1994. Homomeric interactions between type II transforming growth factor-b receptors. J Biol Chem 269: 22868-22874.
    • (1994) J Biol Chem , vol.269 , pp. 22868-22874
    • Chen, R.H.1    Derynck, R.2
  • 30
    • 0030926004 scopus 로고    scopus 로고
    • Mechanism of TGFb receptor inhibition by FKBP12
    • Chen YG, Liu F, Massagué J. 1997. Mechanism of TGFb receptor inhibition by FKBP12. EMBO J 16: 3866-3876.
    • (1997) EMBO J , vol.16 , pp. 3866-3876
    • Chen, Y.G.1    Liu, F.2    Massagué, J.3
  • 31
    • 0032213514 scopus 로고    scopus 로고
    • Transforming growth factor-b type I receptor kinase mutant–associated with metastatic breast cancer
    • Chen TP, Carter D, Garrigue-Antar L, Reiss M. 1998. Transforming growth factor-b type I receptor kinase mutant–associated with metastatic breast cancer. Cancer Res 58: 4805-4810.
    • (1998) Cancer Res , vol.58 , pp. 4805-4810
    • Chen, T.P.1    Carter, D.2    Garrigue-Antar, L.3    Reiss, M.4
  • 32
    • 0035452460 scopus 로고    scopus 로고
    • Novel inactivating mutations of transforming growth factor-b type I receptor gene in head-and-neck cancer metastases
    • Chen T, Yan W, Wells RG, Rimm DL, McNiff J, Leffell D, Reiss M. 2001. Novel inactivating mutations of transforming growth factor-b type I receptor gene in head-and-neck cancer metastases. Int J Cancer 93: 653-661.
    • (2001) Int J Cancer , vol.93 , pp. 653-661
    • Chen, T.1    Yan, W.2    Wells, R.G.3    Rimm, D.L.4    McNiff, J.5    Leffell, D.6    Reiss, M.7
  • 36
    • 55849145475 scopus 로고    scopus 로고
    • Transforming growth factor b-induced Smad1/5 phosphorylation in epithelial cells is mediated by novel receptor complexes and is essential for anchorage-independent growth
    • Daly AC, Randall RA, Hill CS. 2008. Transforming growth factor b-induced Smad1/5 phosphorylation in epithelial cells is mediated by novel receptor complexes and is essential for anchorage-independent growth. Mol Cell Biol 28: 6889-6902.
    • (2008) Mol Cell Biol , vol.28 , pp. 6889-6902
    • Daly, A.C.1    Randall, R.A.2    Hill, C.S.3
  • 37
    • 0033996038 scopus 로고    scopus 로고
    • STRAP and Smad7 synergize in the inhibition of transforming growth factor b signaling
    • Datta PK, Moses HL. 2000. STRAP and Smad7 synergize in the inhibition of transforming growth factor b signaling. Mol Cell Biol 20: 3157-3167.
    • (2000) Mol Cell Biol , vol.20 , pp. 3157-3167
    • Datta, P.K.1    Moses, H.L.2
  • 38
    • 0032567487 scopus 로고    scopus 로고
    • Identification of STRAP, a novel WD domain protein in transforming growth factor-b signaling
    • Datta PK, Chytil A, Gorska AE, Moses HL. 1998. Identification of STRAP, a novel WD domain protein in transforming growth factor-b signaling. J Biol Chem 273: 34671-34674.
    • (1998) J Biol Chem , vol.273 , pp. 34671-34674
    • Datta, P.K.1    Chytil, A.2    Gorska, A.E.3    Moses, H.L.4
  • 39
    • 33847369980 scopus 로고    scopus 로고
    • Identification of BMP9 and BMP10 as functional activators of the orphan activin receptor-like kinase 1 (ALK1) in endothelial cells
    • David L, Mallet C, Mazerbourg S, Feige JJ, Bailly S. 2007. Identification of BMP9 and BMP10 as functional activators of the orphan activin receptor-like kinase 1 (ALK1) in endothelial cells. Blood 109: 1953-1961.
    • (2007) Blood , vol.109 , pp. 1953-1961
    • David, L.1    Mallet, C.2    Mazerbourg, S.3    Feige, J.J.4    Bailly, S.5
  • 40
    • 84859906148 scopus 로고    scopus 로고
    • Key role for ubiquitin protein modification in TGFb signal transduction
    • De Boeck M, ten Dijke P. 2012. Key role for ubiquitin protein modification in TGFb signal transduction. Ups J Med Sci 117: 153-165.
    • (2012) Ups J Med Sci , vol.117 , pp. 153-165
    • De Boeck, M.1    Ten Dijke, P.2
  • 41
    • 57049158952 scopus 로고    scopus 로고
    • ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Derynck R, Miyazono K, ed. 2008. The TGF-β family. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2008) The TGF-β Family
    • Derynck, R.1    Miyazono, K.2
  • 42
    • 0037598870 scopus 로고    scopus 로고
    • Distinct endocytic pathways regulate TGF-β receptor signalling and turnover
    • Di Guglielmo GM, Le Roy C, Goodfellow AF, Wrana JL. 2003. Distinct endocytic pathways regulate TGF-β receptor signalling and turnover. Nat Cell Biol 5: 410-421.
    • (2003) Nat Cell Biol , vol.5 , pp. 410-421
    • Di Guglielmo, G.M.1    Le Roy, C.2    Goodfellow, A.F.3    Wrana, J.L.4
  • 45
    • 0035918274 scopus 로고    scopus 로고
    • Smurf1 interacts with transforming growth factor-b type I receptor through Smad7 and induces receptor degradation
    • Ebisawa T, Fukuchi M, Murakami G, Chiba T, Tanaka K, Imamura T, Miyazono K. 2001. Smurf1 interacts with transforming growth factor-b type I receptor through Smad7 and induces receptor degradation. J Biol Chem 276: 12477-12480.
    • (2001) J Biol Chem , vol.276 , pp. 12477-12480
    • Ebisawa, T.1    Fukuchi, M.2    Murakami, G.3    Chiba, T.4    Tanaka, K.5    Imamura, T.6    Miyazono, K.7
  • 47
    • 33751328068 scopus 로고    scopus 로고
    • Ki26894, a novel transforming growth factor-b type I receptor kinase inhibitor, inhibits in vitro invasion and in vivo bone metastasis of a human breast cancer cell line
    • Ehata S, Hanyu A, Fujime M, Katsuno Y, Fukunaga E, Goto K, Ishikawa Y, Nomura K, Yokoo H, Shimizu T, et al. 2007. Ki26894, a novel transforming growth factor-b type I receptor kinase inhibitor, inhibits in vitro invasion and in vivo bone metastasis of a human breast cancer cell line. Cancer Sci 98: 127-133.
    • (2007) Cancer Sci , vol.98 , pp. 127-133
    • Ehata, S.1    Hanyu, A.2    Fujime, M.3    Katsuno, Y.4    Fukunaga, E.5    Goto, K.6    Ishikawa, Y.7    Nomura, K.8    Yokoo, H.9    Shimizu, T.10
  • 48
    • 84862758806 scopus 로고    scopus 로고
    • Oligomeric interactions of TGF-β and BMP receptors
    • Ehrlich M, Gutman O, Knaus P, Henis YI. 2012. Oligomeric interactions of TGF-β and BMP receptors. FEBS Lett 586: 1885-1896.
    • (2012) FEBS Lett , vol.586 , pp. 1885-1896
    • Ehrlich, M.1    Gutman, O.2    Knaus, P.3    Henis, Y.I.4
  • 50
    • 0037016690 scopus 로고    scopus 로고
    • Betaglycan inhibits TGF-β signaling by preventing type I-type II receptor complex formation. Glycosaminoglycan modifications alter betaglycan function
    • Eickelberg O, Centrella M, Reiss M, Kashgarian M, Wells RG,. 2002. Betaglycan inhibits TGF-β signaling by preventing type I-type II receptor complex formation. Glycosaminoglycan modifications alter betaglycan function. J Biol Chem 277: 823-829.
    • (2002) J Biol Chem , vol.277 , pp. 823-829
    • Eickelberg, O.M.1    Reiss, M.2    Kashgarian, M.3    Wells, R.G.4
  • 51
    • 84905983197 scopus 로고    scopus 로고
    • Ectodomain shedding of TbRIII is required for TbRIII-mediated suppression of TGF-β signaling and breast cancer migration and invasion
    • Elderbroom JL, Huang JJ, Gatza CE, Chen J, How T, Starr M, Nixon AB, Blobe GC. 2014. Ectodomain shedding of TbRIII is required for TbRIII-mediated suppression of TGF-β signaling and breast cancer migration and invasion. Mol Biol Cell 25: 2320-2332.
    • (2014) Mol Biol Cell , vol.25 , pp. 2320-2332
    • Elderbroom, J.L.1    Huang, J.J.2    Gatza, C.E.3    Chen, J.4    How, T.5    Starr, M.6    Nixon, A.B.7    Blobe, G.C.8
  • 52
    • 84874708151 scopus 로고    scopus 로고
    • CCN2/CTGF increases expression of miR-302 microRNAs, which target the TGFβ type II receptor with implications for nephropathic cell phenotypes
    • Faherty N, Curran SP, O’Donovan H, Martin F, Godson C, Brazil DP, Crean JK. 2012. CCN2/CTGF increases expression of miR-302 microRNAs, which target the TGFβ type II receptor with implications for nephropathic cell phenotypes. J Cell Sci 125: 5621-5629.
    • (2012) J Cell Sci , vol.125 , pp. 5621-5629
    • Faherty, N.1    Curran, S.P.2    O’Donovan, H.3    Martin, F.4    Godson, C.5    Brazil, D.P.6    Crean, J.K.7
  • 54
    • 0030926005 scopus 로고    scopus 로고
    • A kinase subdomain of transforming growth factor-b (TGF-β) type I receptor determines the TGF-β intracellular signaling specificity
    • Feng XH, Derynck R. 1997. A kinase subdomain of transforming growth factor-b (TGF-β) type I receptor determines the TGF-β intracellular signaling specificity. EMBO J 16: 3912-3923.
    • (1997) EMBO J , vol.16 , pp. 3912-3923
    • Feng, X.H.1    Derynck, R.2
  • 55
    • 23044466047 scopus 로고    scopus 로고
    • Specificity and versatility in TGF-β signaling through Smads
    • Feng XH, Derynck R. 2005. Specificity and versatility in TGF-β signaling through Smads. Annu Rev Cell Dev Biol 21: 659-693.
    • (2005) Annu Rev Cell Dev Biol , vol.21 , pp. 659-693
    • Feng, X.H.1    Derynck, R.2
  • 56
    • 84855189041 scopus 로고    scopus 로고
    • A miR-125b binding site polymorphism in bone morphogenetic protein membrane receptor type IB gene and prostate cancer risk in China
    • Feng NH, Xu B, Tao J, Li PC, Cheng G, Min ZC, Mi YY, Wang ML, Tong N, Tang JL, et al. 2012. A miR-125b binding site polymorphism in bone morphogenetic protein membrane receptor type IB gene and prostate cancer risk in China. Mol Biol Rep 39: 369-373.
    • (2012) Mol Biol Rep , vol.39 , pp. 369-373
    • Feng, N.H.1    Xu, B.2    Tao, J.3    Li, P.C.4    Cheng, G.5    Min, Z.C.6    Mi, Y.Y.7    Wang, M.L.8    Tong, N.9    Tang, J.L.10
  • 57
    • 78449269819 scopus 로고    scopus 로고
    • The oncoprotein c-ski functions as a direct antagonist of the transforming growth factor-b type I receptor
    • Ferrand N, Atfi A, Prunier C. 2010. The oncoprotein c-ski functions as a direct antagonist of the transforming growth factor-b type I receptor. Cancer Res 70: 8457-8466.
    • (2010) Cancer Res , vol.70 , pp. 8457-8466
    • Ferrand, N.1    Atfi, A.2    Prunier, C.3
  • 58
    • 0037173716 scopus 로고    scopus 로고
    • Yes-associated protein (YAP65) interacts with Smad7 and potentiates its inhibitory activity against TGF-β/Smad signaling
    • Ferrigno O, Lallemand F, Verrecchia F, L’Hoste S, Camonis J, Atfi A, Mauviel A. 2002. Yes-associated protein (YAP65) interacts with Smad7 and potentiates its inhibitory activity against TGF-β/Smad signaling. Oncogene 21: 4879-4884.
    • (2002) Oncogene , vol.21 , pp. 4879-4884
    • Ferrigno, O.1    Lallemand, F.2    Verrecchia, F.3    L’Hoste, S.4    Camonis, J.5    Atfi, A.6    Mauviel, A.7
  • 59
    • 58049195151 scopus 로고    scopus 로고
    • Endocytosis of the type III transforming growth factor-b (TGF-β) receptor through the clathrin-independent/lipid raft path way regulates TGF-β signaling and receptor down-regulation
    • Finger EC, Lee NY, You HJ, Blobe GC. 2008. Endocytosis of the type III transforming growth factor-b (TGF-β) receptor through the clathrin-independent/lipid raft path way regulates TGF-β signaling and receptor down-regulation. J Biol Chem 283: 34808-34818.
    • (2008) J Biol Chem , vol.283 , pp. 34808-34818
    • Finger, E.C.1    Lee, N.Y.2    You, H.J.3    Blobe, G.C.4
  • 62
    • 33747086130 scopus 로고    scopus 로고
    • B3 integrin and Src facilitate transforming growth factor-b mediated induction of epithelial-mesenchymal transition in mammary epithelial cells
    • Galliher AJ, Schiemann WP. 2006. b3 integrin and Src facilitate transforming growth factor-b mediated induction of epithelial-mesenchymal transition in mammary epithelial cells. Breast Cancer Res 8: R42.
    • (2006) Breast Cancer Res , vol.8
    • Galliher, A.J.1
  • 63
    • 34248584887 scopus 로고    scopus 로고
    • Src phosphorylates Tyr284 in TGF-β type II receptor and regulates TGF-β stimulation of p38 MAPK during breast cancer cell proliferation and invasion
    • Galliher AJ, Schiemann WP. 2007. Src phosphorylates Tyr284 in TGF-β type II receptor and regulates TGF-β stimulation of p38 MAPK during breast cancer cell proliferation and invasion. Cancer Res 67: 3752-3758.
    • (2007) Cancer Res , vol.67 , pp. 3752-3758
    • Galliher, A.J.1    Schiemann, W.P.2
  • 64
    • 40549115658 scopus 로고    scopus 로고
    • Grb2 binding to Tyr284 in TbR-II is essential for mammary tumor growth and metastasis stimulated by TGF-β
    • Galliher-Beckley AJ, Schiemann WP. 2008. Grb2 binding to Tyr284 in TbR-II is essential for mammary tumor growth and metastasis stimulated by TGF-β. Carcinogenesis 29: 244-251.
    • (2008) Carcinogenesis , vol.29 , pp. 244-251
    • Galliher-Beckley, A.J.1    Schiemann, W.P.2
  • 65
    • 33751320565 scopus 로고    scopus 로고
    • Inhibition of growth and metastasis of mouse mammary carcinoma by selective inhibitor of transforming growth factor-b type I receptor kinase in vivo
    • Ge R, Rajeev V, Ray P, Lattime E, Rittling S, Medicherla S, Protter A, Murphy A, Chakravarty J, Dugar S, et al. 2006. Inhibition of growth and metastasis of mouse mammary carcinoma by selective inhibitor of transforming growth factor-b type I receptor kinase in vivo. Clin Cancer Res 12: 4315-4330.
    • (2006) Clin Cancer Res , vol.12 , pp. 4315-4330
    • Ge, R.1    Rajeev, V.2    Ray, P.3    Lattime, E.4    Rittling, S.5    Medicherla, S.6    Protter, A.7    Murphy, A.8    Chakravarty, J.9    Dugar, S.10
  • 66
    • 0032559594 scopus 로고    scopus 로고
    • Oligomeric structure of type I and type II transforming growth factor b receptors: Homodimers form in the ER and persist at the plasma membrane
    • Gilboa L, Wells RG, Lodish HF, Henis YI. 1998. Oligomeric structure of type I and type II transforming growth factor b receptors: Homodimers form in the ER and persist at the plasma membrane. J Cell Biol 140: 767-777.
    • (1998) J Cell Biol , vol.140 , pp. 767-777
    • Gilboa, L.1    Wells, R.G.2    Lodish, H.F.3    Henis, Y.I.4
  • 67
    • 84982815952 scopus 로고    scopus 로고
    • Neuropilin-1 is a receptor for latent and active TGFb-1and is involved in suppression by regulatory T cells
    • Glinka Y, Prud’homme GJ. 2008. Neuropilin-1 is a receptor for latent and active TGFb-1and is involved in suppression by regulatory T cells. FASEB J 22: 664.4.
    • (2008) FASEB J , vol.22 , Issue.664
    • Glinka, Y.1    Prud’Homme, G.J.2
  • 68
    • 79953702245 scopus 로고    scopus 로고
    • Neuropilin-1 exerts co-receptor function for TGF-β-1 on the membrane of cancer cells and enhances responses to both latent and active TGF-β
    • Glinka Y, Stoilova S, Mohammed N, Prud’homme GJ. 2011. Neuropilin-1 exerts co-receptor function for TGF-β-1 on the membrane of cancer cells and enhances responses to both latent and active TGF-β. Carcinogenesis 32: 613-621.
    • (2011) Carcinogenesis , vol.32 , pp. 613-621
    • Glinka, Y.1    Stoilova, S.2    Mohammed, N.3    Prud’Homme, G.J.4
  • 69
    • 34547122921 scopus 로고    scopus 로고
    • Selective inhibitory effects of Smad6 on bone morphogenetic protein type I receptors
    • Goto K, Kamiya Y, Imamura T, Miyazono K, Miyazawa K. 2007. Selective inhibitory effects of Smad6 on bone morphogenetic protein type I receptors. J Biol Chem 282: 20603-20611.
    • (2007) J Biol Chem , vol.282 , pp. 20603-20611
    • Goto, K.1    Kamiya, Y.2    Imamura, T.3    Miyazono, K.4    Miyazawa, K.5
  • 71
    • 33845465701 scopus 로고    scopus 로고
    • Cripto binds transforming growth factor b (TGF-β) and inhibits TGF-β signaling
    • Gray PC, Shani G, Aung K, Kelber J, Vale W. 2006. Cripto binds transforming growth factor b (TGF-β) and inhibits TGF-β signaling. Mol Cell Biol 26: 9268-9278.
    • (2006) Mol Cell Biol , vol.26 , pp. 9268-9278
    • Gray, P.C.1    Shani, G.2    Aung, K.3    Kelber, J.4    Vale, W.5
  • 72
    • 0031741865 scopus 로고    scopus 로고
    • Physical and functional interactions between type I transforming growth factor b receptors and Ba, a WD-40 repeat subunit of phosphatase 2A
    • Griswold-Prenner I, Kamibayashi C, Maruoka EM, Mumby MC, Derynck R. 1998. Physical and functional interactions between type I transforming growth factor b receptors and Ba, a WD-40 repeat subunit of phosphatase 2A. Mol Cell Biol 18: 6595-6604.
    • (1998) Mol Cell Biol , vol.18 , pp. 6595-6604
    • Griswold-Prenner, I.1    Kamibayashi, C.2    Maruoka, E.M.3    Mumby, M.C.4    Derynck, R.5
  • 74
    • 0035141917 scopus 로고    scopus 로고
    • Bambi is coexpressed with BMP-4 during mouse embryogenesis
    • Grotewold L, Plum M, Dildrop R, Peters T, Ruther U. 2001. Bambi is coexpressed with BMP-4 during mouse embryogenesis. Mech Dev 100: 327-330.
    • (2001) Mech Dev , vol.100 , pp. 327-330
    • Grotewold, L.1    Plum, M.2    Dildrop, R.3    Peters, T.4    Ruther, U.5
  • 75
    • 84892389396 scopus 로고    scopus 로고
    • TRAF6 stimulates the tumor-promoting effects of TGFb type I receptor through polyubiquitination and activation of presenilin 1
    • Gudey SK, Sundar R, Mu Y, Wallenius A, Zang G, Bergh A, Heldin CH, Landstrom M. 2014. TRAF6 stimulates the tumor-promoting effects of TGFb type I receptor through polyubiquitination and activation of presenilin 1. Sci Signa l 7: ra2.
    • (2014) Sci Signa , vol.1 , Issue.7
    • Gudey, S.K.1    Sundar, R.2    Mu, Y.3    Wallenius, A.4    Zang, G.5    Bergh, A.6    Heldin, C.H.7    Landstrom, M.8
  • 76
    • 0037047426 scopus 로고    scopus 로고
    • Extracellular and cytoplasmic domains of endoglin interact with the transforming growth factor-b receptors I and II
    • Guerrero-Esteo M, Sanchez-Elsner T, Letamendia A, Bernabeu C. 2002. Extracellular and cytoplasmic domains of endoglin interact with the transforming growth factor-b receptors I and II. J Biol Chem 277: 29197-29209.
    • (2002) J Biol Chem , vol.277 , pp. 29197-29209
    • Guerrero-Esteo, M.1    Sanchez-Elsner, T.2    Letamendia, A.3    Bernabeu, C.4
  • 82
    • 0037144841 scopus 로고    scopus 로고
    • TGF b receptor internalization into EEA1-enriched early endosomes: Role in signaling to Smad2
    • Hayes S, Chawla A, Corvera S. 2002. TGF b receptor internalization into EEA1-enriched early endosomes: Role in signaling to Smad2. J Cell Biol 158: 1239-1249.
    • (2002) J Cell Biol , vol.158 , pp. 1239-1249
    • Hayes, S.1    Chawla, A.2    Corvera, S.3
  • 84
    • 84982781486 scopus 로고    scopus 로고
    • Signals and receptors
    • (ed. Cantley LC, Hunter T, Sever R, Thorner J, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • Heldin CH, Lu B, Evans R, Gutkind S. 2014. Signals and receptors. In Signal transduction principles, pathways and processes (ed. Cantley LC, Hunter T, Sever R, Thorner J), pp. 3-29. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
    • (2014) Signal Transduction Principles, Pathways and Processes , pp. 3-29
    • Heldin, C.H.1    Lu, B.2    Evans, R.3    Gutkind, S.4
  • 85
    • 0028291369 scopus 로고
    • The types II and III transforming growth factor-b receptors form homo-oligomers
    • Henis YI, Moustakas A, Lin HY, Lodish HF. 1994. The types II and III transforming growth factor-b receptors form homo-oligomers. J Cell Biol 126: 139-154.
    • (1994) J Cell Biol , vol.126 , pp. 139-154
    • Henis, Y.I.1    Moustakas, A.2    Lin, H.Y.3    Lodish, H.F.4
  • 86
    • 84904489086 scopus 로고    scopus 로고
    • The emerging roles of deubiquitylating enzymes (DUBs) in the TGFb and BMP pathways
    • Herhaus L, Sapkota GP. 2014. The emerging roles of deubiquitylating enzymes (DUBs) in the TGFb and BMP pathways. Cell Signal 26: 2186-2192.
    • (2014) Cell Signal , vol.26 , pp. 2186-2192
    • Herhaus, L.1    Sapkota, G.P.2
  • 88
    • 0035355473 scopus 로고    scopus 로고
    • The adaptor molecule disabled-2 links the transforming growth factor β receptors to the Smad pathway
    • Hocevar BA, Smine A, Xu XX, Howe PH. 2001. The adaptor molecule disabled-2 links the transforming growth factor β receptors to the Smad pathway. EMBO J 20: 2789-2801.
    • (2001) EMBO J , vol.20 , pp. 2789-2801
    • Hocevar, B.A.1    Smine, A.2    Xu, X.X.3    Howe, P.H.4
  • 89
    • 78649726867 scopus 로고    scopus 로고
    • Quantitative analysis of TGFBR2 mutations in Marfan-syndrome-related disorders suggests a correlation between phenotypic severity and Smad signaling activity
    • Horbelt D, Guo G, Robinson PN, Knaus P. 2010. Quantitative analysis of TGFBR2 mutations in Marfan-syndrome-related disorders suggests a correlation between phenotypic severity and Smad signaling activity. J Cell Sci 123: 4340-4350.
    • (2010) J Cell Sci , vol.123 , pp. 4340-4350
    • Horbelt, D.1    Guo, G.2    Robinson, P.N.3    Knaus, P.4
  • 95
    • 0033524943 scopus 로고    scopus 로고
    • Crystal structure of the cytoplasmic domain of the type I TGF b receptor in complex with FKBP12
    • Huse M, Chen YG, Massagué J, Kuriyan J. 1999. Crystal structure of the cytoplasmic domain of the type I TGF b receptor in complex with FKBP12. Cell 96: 425-436.
    • (1999) Cell , vol.96 , pp. 425-436
    • Huse, M.1    Chen, Y.G.2    Massagué, J.3    Kuriyan, J.4
  • 96
    • 0034796457 scopus 로고    scopus 로고
    • The TGF b receptor activation process: An inhibitor-to substrate-binding switch
    • Huse M, Muir TW, Xu L, Chen YG, Kuriyan J, Massagué J. 2001. The TGF b receptor activation process: An inhibitor-to substrate-binding switch. Mol Cell 8: 671-682.
    • (2001) Mol Cell , vol.8 , pp. 671-682
    • Huse, M.1    Muir, T.W.2    Xu, L.3    Chen, Y.G.4    Kuriyan, J.5    Massagué, J.6
  • 98
    • 0034093738 scopus 로고    scopus 로고
    • Smad6 is a Smad1/5-induced Smad inhibitor. Characterization of bone morphogenetic protein-responsive element in the mouse Smad6 promoter
    • Ishida W, Hamamoto T, Kusanagi K, Yagi K, Kawabata M, Takehara K, Sampath TK, Kato M, Miyazono K. 2000. Smad6 is a Smad1/5-induced Smad inhibitor. Characterization of bone morphogenetic protein-responsive element in the mouse Smad6 promoter. J Biol Chem 275: 6075-6079.
    • (2000) J Biol Chem , vol.275 , pp. 6075-6079
    • Ishida, W.1    Hamamoto, T.2    Kusanagi, K.3    Yagi, K.4    Kawabata, M.5    Takehara, K.6    Sampath, T.K.7    Kato, M.8    Miyazono, K.9
  • 99
    • 33646713486 scopus 로고    scopus 로고
    • The TGF b activated kinase TAK1 regulates vascular development in vivo
    • Jadrich JL, O’Connor MB, Coucouvanis E. 2006. The TGF b activated kinase TAK1 regulates vascular development in vivo. Development 133: 1529-1541.
    • (2006) Development , vol.133 , pp. 1529-1541
    • Jadrich, J.L.1    O’Connor, M.B.2    Coucouvanis, E.3
  • 101
    • 34547105808 scopus 로고    scopus 로고
    • Requirement for the dynein light chain km23-1 in a Smad2-dependent transforming growth factor-b signaling pathway
    • Jin Q, Ding W, Mulder KM. 2007a. Requirement for the dynein light chain km23-1 in a Smad2-dependent transforming growth factor-b signaling pathway. J Biol Chem 282: 19122-19132.
    • (2007) J Biol Chem , vol.282 , pp. 19122-19132
    • Jin, Q.1    Ding, W.2    Mulder, K.M.3
  • 102
    • 35448957195 scopus 로고    scopus 로고
    • TrkC binds to the bone morphogenetic protein type II receptor to suppress bone morphogenetic protein signaling
    • Jin W, Yun C, Kim HS, Kim SJ. 2007b. TrkC binds to the bone morphogenetic protein type II receptor to suppress bone morphogenetic protein signaling. Cancer Res 67: 9869-9877.
    • (2007) Cancer Res , vol.67 , pp. 9869-9877
    • Jin, W.1    Yun, C.2    Kim, H.S.3    Kim, S.J.4
  • 103
    • 36849008767 scopus 로고    scopus 로고
    • TrkC binds to the type II TGF-β receptor to suppress TGF-β signaling
    • Jin W, Yun C, Kwak MK, Kim TA, Kim SJ. 2007c. TrkC binds to the type II TGF-β receptor to suppress TGF-β signaling. Oncogene 26: 7684-7691.
    • (2007) Oncogene , vol.26 , pp. 7684-7691
    • Jin, W.1    Yun, C.2    Kwak, M.K.3    Kim, T.A.4    Kim, S.J.5
  • 104
    • 84864386292 scopus 로고    scopus 로고
    • The TGFb receptor-interacting protein km23-1/DYNLRB1 plays an adaptor role in TGFb1 autoinduction via its association with Ras
    • Jin QY, Ding W, Mulder KM. 2012. The TGFb receptor-interacting protein km23-1/DYNLRB1 plays an adaptor role in TGFb1 autoinduction via its association with Ras. J Biol Chem 287: 26453-26463.
    • (2012) J Biol Chem , vol.287 , pp. 26453-26463
    • Jin, Q.Y.1    Ding, W.2    Mulder, K.M.3
  • 106
    • 77957267462 scopus 로고    scopus 로고
    • Smad7 inhibits transforming growth factor-b family type I receptors through two distinct modes of interaction
    • Kamiya Y, Miyazono K, Miyazawa K. 2010. Smad7 inhibits transforming growth factor-b family type I receptors through two distinct modes of interaction. J Biol Chem 285: 30804-30813.
    • (2010) J Biol Chem , vol.285 , pp. 30804-30813
    • Kamiya, Y.1    Miyazono, K.2    Miyazawa, K.3
  • 108
    • 44649163272 scopus 로고    scopus 로고
    • The type I TGF-β receptor is covalently modified and regulated by sumoylation
    • Kang JS, Saunier EF, Akhurst RJ, Derynck R. 2008. The type I TGF-β receptor is covalently modified and regulated by sumoylation. Nat Cell Biol 10: 654-664.
    • (2008) Nat Cell Biol , vol.10 , pp. 654-664
    • Kang, J.S.1    Saunier, E.F.2    Akhurst, R.J.3    Derynck, R.4
  • 109
    • 84869041413 scopus 로고    scopus 로고
    • Inhibition of MicroRNA-302 (MiR-302) by bone morphogenetic protein 4 (BMP4) facilitates the BMP signaling pathway
    • Kang H, Louie J, Weisman A, Sheu-Gruttadauria J, Davis-Dusenbery BN, Lagna G, Hata A. 2012. Inhibition of MicroRNA-302 (miR-302) by bone morphogenetic protein 4 (BMP4) facilitates the BMP signaling pathway. J Biol Chem 287: 38656-38664.
    • (2012) J Biol Chem , vol.287 , pp. 38656-38664
    • Kang, H.1    Louie, J.2    Weisman, A.3    Sheu-Gruttadauria, J.4    Davis-Dusenbery, B.N.5    Lagna, G.6    Hata, A.7
  • 113
    • 0034517389 scopus 로고    scopus 로고
    • Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGFβ receptor for degradation
    • Kavsak P, Rasmussen RK, Causing CG, Bonni S, Zhu H, Thomsen GH, Wrana JL. 2000. Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGFβ receptor for degradation. Mol Cell 6: 1365-1375.
    • (2000) Mol Cell , vol.6 , pp. 1365-1375
    • Kavsak, P.1    Rasmussen, R.K.2    Causing, C.G.3    Bonni, S.4    Zhu, H.5    Thomsen, G.H.6    Wrana, J.L.7
  • 114
  • 115
    • 69249131695 scopus 로고    scopus 로고
    • Transforming growth factor-b (TGF-β1) activates TAK1 via TAB1-mediated autophosphorylation, independent of TGF-β receptor kinase activity in mesangial cells
    • Kim SI, Kwak JH, Na HJ, Kim JK, Ding Y, Choi ME. 2009. Transforming growth factor-b (TGF-β1) activates TAK1 via TAB1-mediated autophosphorylation, independent of TGF-β receptor kinase activity in mesangial cells. J Biol Chem 284: 22285-22296.
    • (2009) J Biol Chem , vol.284 , pp. 22285-22296
    • Kim, S.I.1    Kwak, J.H.2    Na, H.J.3    Kim, J.K.4    Ding, Y.5    Choi, M.E.6
  • 116
    • 43149095145 scopus 로고    scopus 로고
    • Bone morphogenetic proteins signal through the transforming growth factor-b type III receptor
    • Kirkbride KC, Townsend TA, Bruinsma MW, Barnett JV, Blobe GC. 2008. Bone morphogenetic proteins signal through the transforming growth factor-b type III receptor. J Biol Chem 283: 7628-7637.
    • (2008) J Biol Chem , vol.283 , pp. 7628-7637
    • Kirkbride, K.C.1    Townsend, T.A.2    Bruinsma, M.W.3    Barnett, J.V.4    Blobe, G.C.5
  • 117
    • 0034043106 scopus 로고    scopus 로고
    • Crystal structure of the BMP-2-BRIA ectodomain complex
    • Kirsch T, Sebald W, Dreyer MK. 2000. Crystal structure of the BMP-2-BRIA ectodomain complex. Nat Struct Biol 7: 492-496.
    • (2000) Nat Struct Biol , vol.7 , pp. 492-496
    • Kirsch, T.1    Sebald, W.2    Dreyer, M.K.3
  • 119
    • 41949085434 scopus 로고    scopus 로고
    • Structure analysis of bone morphogenetic protein-2 type I receptor complexes reveals a mechanism of receptor inactivation in juvenile polyposis syndrome
    • Kotzsch A, Nickel J, Seher A, Heinecke K, van Geersdaele L, Herrmann T, Sebald W, Mueller TD. 2008. Structure analysis of bone morphogenetic protein-2 type I receptor complexes reveals a mechanism of receptor inactivation in juvenile polyposis syndrome. J Biol Chem 283: 5876-5887.
    • (2008) J Biol Chem , vol.283 , pp. 5876-5887
    • Kotzsch, A.1    Nickel, J.2    Seher, A.3    Heinecke, K.4    Van Geersdaele, L.5    Herrmann, T.6    Sebald, W.7    Mueller, T.D.8
  • 121
    • 2942536704 scopus 로고    scopus 로고
    • Id2 and Id3 define the potency of cell proliferation and differentiation responses to transforming growth factor β and bone morphogenetic protein
    • Kowanetz M, Valcourt U, Bergström R, Heldin CH, Moustakas A. 2004. Id2 and Id3 define the potency of cell proliferation and differentiation responses to transforming growth factor β and bone morphogenetic protein. Mol Cell Biol 24: 4241-4254.
    • (2004) Mol Cell Biol , vol.24 , pp. 4241-4254
    • Kowanetz, M.1    Valcourt, U.2    Bergström, R.3    Heldin, C.H.4    Moustakas, A.5
  • 123
    • 50349094328 scopus 로고    scopus 로고
    • BAT3 interacts with transforming growth factor-b (TGF-β) receptors and enhances TGF-β1-induced type I collagen expression in mesangial cells
    • Kwak JH, Kim SI, Kim JK, Choi ME. 2008. BAT3 interacts with transforming growth factor-b (TGF-β) receptors and enhances TGF-β1-induced type I collagen expression in mesangial cells. J Biol Chem 283: 19816-19825.
    • (2008) J Biol Chem , vol.283 , pp. 19816-19825
    • Kwak, J.H.1    Kim, S.I.2    Kim, J.K.3    Choi, M.E.4
  • 124
    • 0030978105 scopus 로고    scopus 로고
    • The type II transforming growth factor-b receptor autophosphorylates not only on serine and threonine but also on tyrosine residues
    • Lawler S, Feng XH, Chen RH, Maruoka EM, Turck CW, Griswold-Prenner I, Derynck R. 1997. The type II transforming growth factor-b receptor autophosphorylates not only on serine and threonine but also on tyrosine residues. J Biol Chem 272: 14850-14859.
    • (1997) J Biol Chem , vol.272 , pp. 14850-14859
    • Lawler, S.1    Feng, X.H.2    Chen, R.H.3    Maruoka, E.M.4    Turck, C.W.5    Griswold-Prenner, I.6    Derynck, R.7
  • 127
    • 57749084578 scopus 로고    scopus 로고
    • Endoglin promotes transforming growth factor b-mediated Smad 1/5/8 signaling and inhibits endothelial cell migration through its association with GIPC
    • Lee NY, Ray B, How T, Blobe GC. 2008. Endoglin promotes transforming growth factor b-mediated Smad 1/5/8 signaling and inhibits endothelial cell migration through its association with GIPC. J Biol Chem 283: 32527-32533.
    • (2008) J Biol Chem , vol.283 , pp. 32527-32533
    • Lee, N.Y.1    Ray, B.2    How, T.3    Blobe, G.C.4
  • 128
    • 70350088248 scopus 로고    scopus 로고
    • The transforming growth factor-b type III receptor mediates distinct subcellular trafficking and downstream signaling of activin-like kinase (ALK)3 and ALK6 receptors
    • Lee NY, Kirkbride KC, Sheu RD, Blobe GC. 2009. The transforming growth factor-b type III receptor mediates distinct subcellular trafficking and downstream signaling of activin-like kinase (ALK)3 and ALK6 receptors. Mol Biol Cell 20: 4362-4370.
    • (2009) Mol Biol Cell , vol.20 , pp. 4362-4370
    • Lee, N.Y.1    Kirkbride, K.C.2    Sheu, R.D.3    Blobe, G.C.4
  • 129
    • 11244313831 scopus 로고    scopus 로고
    • Activation of LIMK1 by binding to the BMP receptor, BMPRII, regulates BMP-dependent dendritogenesis
    • Lee-Hoeflich ST, Causing CG, Podkowa M, Zhao X, Wrana JL, Attisano L. 2004. Activation of LIMK1 by binding to the BMP receptor, BMPRII, regulates BMP-dependent dendritogenesis. EMBO J 23: 4792-4801.
    • (2004) EMBO J , vol.23 , pp. 4792-4801
    • Lee-Hoeflich, S.T.1    Causing, C.G.2    Podkowa, M.3    Zhao, X.4    Wrana, J.L.5    Attisano, L.6
  • 132
    • 84921451313 scopus 로고    scopus 로고
    • Regulatory MiR-148a-ACVR1/BMP circuit defines a cancer stem cell-like aggressive subtype of hepatocellular carcinoma
    • Li L, Liu YX, Guo Y, Liu B, Zhao YR, Li P, Song FJ, Zheng H, Yu JP, Song TQ, et al. 2015. Regulatory MiR-148a-ACVR1/BMP circuit defines a cancer stem cell-like aggressive subtype of hepatocellular carcinoma. Hepatology 61: 574-584.
    • (2015) Hepatology , vol.61 , pp. 574-584
    • Li, L.1    Liu, Y.X.2    Guo, Y.3    Liu, B.4    Zhao, Y.R.5    Li, P.6    Song, F.J.7    Zheng, H.8    Yu, J.P.9    Song, T.Q.10
  • 133
    • 0036493793 scopus 로고    scopus 로고
    • Cell surface antigen CD109 is a novel member of the a2 macroglobulin/C3, C4, C5 family of thioester-containing proteins
    • Lin M, Sutherland DR, Horsfall W, Totty N, Yeo E, Nayar R, Wu XF, Schuh AC. 2002. Cell surface antigen CD109 is a novel member of the a2 macroglobulin/C3, C4, C5 family of thioester-containing proteins. Blood 99: 1683-1691.
    • (2002) Blood , vol.99 , pp. 1683-1691
    • Lin, M.1    Sutherland, D.R.2    Horsfall, W.3    Totty, N.4    Yeo, E.5    Nayar, R.6    Wu, X.F.7    Schuh, A.C.8
  • 134
    • 4544256756 scopus 로고    scopus 로고
    • Cytoplasmic PML function in TGF-β signalling
    • Lin HK, Bergmann S, Pandolfi PP. 2004. Cytoplasmic PML function in TGF-β signalling. Nature 431: 205-211.
    • (2004) Nature , vol.431 , pp. 205-211
    • Lin, H.K.1    Bergmann, S.2    Pandolfi, P.P.3
  • 135
    • 0032532673 scopus 로고    scopus 로고
    • Transforming growth factor b signaling through smad1 in human breast cancer cells
    • Liu XJ, Yue JB, Frey RS, Zhu QC, Mulder KM. 1998. Transforming growth factor b signaling through smad1 in human breast cancer cells. Cancer Res 58: 4752-4757.
    • (1998) Cancer Res , vol.58 , pp. 4752-4757
    • Liu, X.J.1    Yue, J.B.2    Frey, R.S.3    Zhu, Q.C.4    Mulder, K.M.5
  • 136
    • 67649664111 scopus 로고    scopus 로고
    • TACE-mediated ectodomain shedding of the type I TGF-β receptor downregulates TGF-β signaling
    • Liu C, Xu P, Lamouille S, Xu J, Derynck R. 2009a. TACE-mediated ectodomain shedding of the type I TGF-β receptor downregulates TGF-β signaling. Mol Cell 35: 26-36.
    • (2009) Mol Cell , vol.35 , pp. 26-36
    • Liu, C.1    Xu, P.2    Lamouille, S.3    Xu, J.4    Derynck, R.5
  • 137
    • 58749089988 scopus 로고    scopus 로고
    • TGFb-stimulated Smad1/5 phosphorylation requires the ALK5 L45 loop and mediates the pro-migratory TGFb switch
    • Liu IM, Schilling SH, Knouse KA, Choy L, Derynck R, Wang XF. 2009b. TGFb-stimulated Smad1/5 phosphorylation requires the ALK5 L45 loop and mediates the pro-migratory TGFb switch. EMBO J 28: 88-98.
    • (2009) EMBO J , vol.28 , pp. 88-98
    • Liu, I.M.1    Schilling, S.H.2    Knouse, K.A.3    Choy, L.4    Derynck, R.5    Wang, X.F.6
  • 139
    • 84887069887 scopus 로고    scopus 로고
    • Dragon (Repulsive guidance molecule RGMb) inhibits E-cadherin expression and induces apoptosis in renal tubular epithelial cells
    • Liu WJ, Li XL, Zhao YS, Meng XM, Wan C, Yang BX, Lan HY, Lin HY, Xia Y. 2013. Dragon (repulsive guidance molecule RGMb) inhibits E-cadherin expression and induces apoptosis in renal tubular epithelial cells. J Biol Chem 288: 31528-31539.
    • (2013) J Biol Chem , vol.288 , pp. 31528-31539
    • Liu, W.J.1    Li, X.L.2    Zhao, Y.S.3    Meng, X.M.4    Wan, C.5    Yang, B.X.6    Lan, H.Y.7    Lin, H.Y.8    Xia, Y.9
  • 140
    • 84937485159 scopus 로고    scopus 로고
    • SPSB1, a novel negative regulator of the transforming growth factor-b signaling pathway targeting the type II receptor
    • Liu S, Nheu T, Luwor R, Nicholson SE, Zhu HJ. 2015. SPSB1, a novel negative regulator of the transforming growth factor-b signaling pathway targeting the type II receptor. J Biol Chem 290: 17894-17908.
    • (2015) J Biol Chem , vol.290 , pp. 17894-17908
    • Liu, S.1    Nheu, T.2    Luwor, R.3    Nicholson, S.E.4    Zhu, H.J.5
  • 141
    • 0032481351 scopus 로고    scopus 로고
    • The L3 loop: A structural motif determining specific interactions between SMAD proteins and TGF-β receptors
    • Lo RS, Chen YG, Shi Y, Pavletich NP, Massagué J. 1998. The L3 loop: A structural motif determining specific interactions between SMAD proteins and TGF-β receptors. EMBO J 17: 996-1005.
    • (1998) EMBO J , vol.17 , pp. 996-1005
    • Lo, R.S.1    Chen, Y.G.2    Shi, Y.3    Pavletich, N.P.4    Massagué, J.5
  • 145
    • 0027276765 scopus 로고
    • Betaglycan presents ligand to the TGF-β signaling receptor
    • López-Casillas F, Wrana JL, Massagué J. 1993. Betaglycan presents ligand to the TGF-β signaling receptor. Cell 73: 1435-1444.
    • (1993) Cell , vol.73 , pp. 1435-1444
    • López-Casillas, F.1    Wrana, J.L.2    Massagué, J.3
  • 146
    • 0027976511 scopus 로고
    • Betaglycan can act as a dual modulator of TGF-β access to signaling receptors: Mapping of ligand binding and GAG attachment sites
    • López-Casillas F, Payne HM, Andres JL, Massagué J. 1994. Betaglycan can act as a dual modulator of TGF-β access to signaling receptors: Mapping of ligand binding and GAG attachment sites. J Cell Biol 124: 557-568.
    • (1994) J Cell Biol , vol.124 , pp. 557-568
    • López-Casillas, F.1    Payne, H.M.2    Res, J.L.3    Massagué, J.4
  • 148
    • 0842281496 scopus 로고    scopus 로고
    • Ski and SnoN: Negative regulators of TGF-β signaling
    • Luo K. 2004. Ski and SnoN: Negative regulators of TGF-β signaling. Curr Opin Genet Dev 14: 65-70.
    • (2004) Curr Opin Genet Dev , vol.14 , pp. 65-70
    • Luo, K.1
  • 149
    • 0030972496 scopus 로고    scopus 로고
    • Positive and negative regulation of type II TGFb receptor signal transduction by autophos-phorylation on multiple serine residues
    • Luo KX, Lodish HF. 1997. Positive and negative regulation of type II TGFb receptor signal transduction by autophos-phorylation on multiple serine residues. EMBO J 16: 1970-1981.
    • (1997) EMBO J , vol.16 , pp. 1970-1981
    • Luo, K.X.1    Lodish, H.F.2
  • 150
    • 84896545297 scopus 로고    scopus 로고
    • Crosstalk between TGF-β/Smad3 and BMP/BMPR2 signaling pathways via miR-17-92 cluster in carotid artery restenosis
    • Luo T, Cui SJ, Bian CJ, Yu XC. 2014. Crosstalk between TGF-β/Smad3 and BMP/BMPR2 signaling pathways via miR-17-92 cluster in carotid artery restenosis. Mol Cell Biochem 389: 169-176.
    • (2014) Mol Cell Biochem , vol.389 , pp. 169-176
    • Luo, T.1    Cui, S.J.2    Bian, C.J.3    Yu, X.C.4
  • 152
    • 1442313955 scopus 로고    scopus 로고
    • Endogenous TGF-β signaling suppresses maturation of osteoblastic mesenchymal cells
    • Maeda S, Hayashi M, Komiya S, Imamura T, Miyazono K. 2004. Endogenous TGF-β signaling suppresses maturation of osteoblastic mesenchymal cells. EMBO J 23: 552-563.
    • (2004) EMBO J , vol.23 , pp. 552-563
    • Maeda, S.1    Hayashi, M.2    Komiya, S.3    Imamura, T.4    Miyazono, K.5
  • 154
    • 84894268985 scopus 로고    scopus 로고
    • MiR-17 regulates the proliferation and differentiation of the neural precursor cells during mouse corticogenesis
    • Mao SS, Li HQ, Sun Q, Zen K, Zhang CY, Li L. 2014. miR-17 regulates the proliferation and differentiation of the neural precursor cells during mouse corticogenesis. FEBS J 281: 1144-1158.
    • (2014) FEBS J , vol.281 , pp. 1144-1158
    • Mao, S.S.1    Li, H.Q.2    Sun, Q.3    Zen, K.4    Zhang, C.Y.5    Li, L.6
  • 156
    • 84866742560 scopus 로고    scopus 로고
    • TGFb signalling in context
    • Massagué J. 2012. TGFb signalling in context. Nat Rev Mol Cell Biol 13: 616-630.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 616-630
    • Massagué, J.1
  • 159
    • 71549129301 scopus 로고    scopus 로고
    • Betaglycan has two independent domains required for high affinity TGF-β binding: Proteolytic cleavage separates the domains and inactivates the neutralizing activity of the soluble receptor
    • Mendoza V, Vilchis-Landeros MM, Mendoza-Hernandez G, Huang T, Villarreal MM, Hinck AP, Lopez-Casillas F, Montiel JL. 2009. Betaglycan has two independent domains required for high affinity TGF-β binding: Proteolytic cleavage separates the domains and inactivates the neutralizing activity of the soluble receptor. Biochemistry 48: 11755-11765.
    • (2009) Biochemistry , vol.48 , pp. 11755-11765
    • Mendoza, V.1    Vilchis-Landeros, M.M.2    Mendoza-Hernandez, G.3    Huang, T.4    Villarreal, M.M.5    Hinck, A.P.6    Lopez-Casillas, F.7    Montiel, J.L.8
  • 160
    • 33845981092 scopus 로고    scopus 로고
    • Identification of Tctex2b, a novel dynein light chain family member that interacts with different transforming growth factor-b receptors
    • Meng Q, Lux A, Holloschi A, Li J, Hughes JM, Foerg T, McCarthy JE, Heagerty AM, Kioschis P, Hafner M, et al. 2006. Identification of Tctex2b, a novel dynein light chain family member that interacts with different transforming growth factor-b receptors. J Biol Chem 281: 37069-37080.
    • (2006) J Biol Chem , vol.281 , pp. 37069-37080
    • Meng, Q.1    Lux, A.2    Holloschi, A.3    Li, J.4    Hughes, J.M.5    Foerg, T.6    McCarthy, J.E.7    Heagerty, A.M.8    Kioschis, P.9    Hafner, M.10
  • 162
    • 84905216761 scopus 로고    scopus 로고
    • Role of TGF-β receptor III localization in polarity and breast cancer progression
    • Meyer AE, Gatza CE, How T, Starr M, Nixon AB, Blobe GC. 2014. Role of TGF-β receptor III localization in polarity and breast cancer progression. Mol Biol Cell 25: 2291-2304.
    • (2014) Mol Biol Cell , vol.25 , pp. 2291-2304
    • Meyer, A.E.1    Gatza, C.E.2    How, T.3    Starr, M.4    Nixon, A.B.5    Blobe, G.C.6
  • 163
    • 4344606636 scopus 로고    scopus 로고
    • Ligand-dependent and -independent transforming growth factor-b receptor recycling regulated by clathrin-mediated endocytosis and Rab11
    • Mitchell H, Choudhury A, Pagano RE, Leof EB. 2004. Ligand-dependent and -independent transforming growth factor-b receptor recycling regulated by clathrin-mediated endocytosis and Rab11. Mol Biol Cell 15: 4166-4178.
    • (2004) Mol Biol Cell , vol.15 , pp. 4166-4178
    • Mitchell, H.1    Choudhury, A.2    Pagano, R.E.3    Leof, E.B.4
  • 164
    • 75649127963 scopus 로고    scopus 로고
    • Bone morphogenetic protein receptors and signal transduction
    • Miyazono K, Kamiya Y, Morikawa M. 2010. Bone morphogenetic protein receptors and signal transduction. J Biochem 147: 35-51.
    • (2010) J Biochem , vol.147 , pp. 35-51
    • Miyazono, K.1    Kamiya, Y.2    Morikawa, M.3
  • 167
    • 24944497786 scopus 로고    scopus 로고
    • Non-Smad TGF-β signals
    • Moustakas A, Heldin CH. 2005. Non-Smad TGF-β signals. J Cell Sci 118: 3573-3584.
    • (2005) J Cell Sci , vol.118 , pp. 3573-3584
    • Moustakas, A.1    Heldin, C.H.2
  • 168
    • 70450187617 scopus 로고    scopus 로고
    • The regulation of TGFβ signal transduction
    • Moustakas A, Heldin CH. 2009. The regulation of TGFβ signal transduction. Development 136: 3699-3714.
    • (2009) Development , vol.136 , pp. 3699-3714
    • Moustakas, A.1    Heldin, C.H.2
  • 169
    • 0027490673 scopus 로고
    • The transforming growth factor b receptors types I, II, and III form hetero-oligomeric complexes in the presence of ligand
    • Moustakas A, Lin HY, Henis YI, Plamondon J, O’Connor-McCourt MD, Lodish HF. 1993. The transforming growth factor b receptors types I, II, and III form hetero-oligomeric complexes in the presence of ligand. J Biol Chem 268: 22215-22218.
    • (1993) J Biol Chem , vol.268 , pp. 22215-22218
    • Moustakas, A.1    Lin, H.Y.2    Henis, Y.I.3    Plamondon, J.4    O’connor-McCourt, M.D.5    Lodish, H.F.6
  • 171
    • 84870814111 scopus 로고    scopus 로고
    • The role of the 30 UTR region in the regulation of the ACVR1/Alk-2 gene expression
    • Mura M, Cappato S, Giacopelli F, Ravazzolo R, Bocciardi R. 2012. The role of the 30 UTR region in the regulation of the ACVR1/Alk-2 gene expression. PLoS ONE 7: e50958.
    • (2012) Plos ONE , vol.7
    • Mura, M.1    Cappato, S.2    Giacopelli, F.3    Ravazzolo, R.4    Bocciardi, R.5
  • 173
    • 34948902740 scopus 로고    scopus 로고
    • A unique element in the cytoplasmic tail of the type II transforming growth factor-b receptor controls basolateral delivery
    • Murphy SJ, Shapira KE, Henis YI, Leof EB. 2007. A unique element in the cytoplasmic tail of the type II transforming growth factor-b receptor controls basolateral delivery. Mol Biol Cell 18: 3788-3799.
    • (2007) Mol Biol Cell , vol.18 , pp. 3788-3799
    • Murphy, S.J.1    Shapira, K.E.2    Henis, Y.I.3    Leof, E.B.4
  • 174
    • 66249141288 scopus 로고    scopus 로고
    • The type III TGF-β receptor regulates epithelial and cancer cell migration through β-arrestin2-mediated activation of Cdc42
    • Mythreye K, Blobe GC. 2009. The type III TGF-β receptor regulates epithelial and cancer cell migration through β-arrestin2-mediated activation of Cdc42. Proc Natl Acad Sci 106: 8221-8226.
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 8221-8226
    • Mythreye, K.1    Blobe, G.C.2
  • 177
    • 69249126664 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis protein and its E3 ligase activity promote transforming growth factor-β-mediated nuclear factor-kB activation during breast cancer progression
    • Neil JR, Tian M, Schiemann WP. 2009. X-linked inhibitor of apoptosis protein and its E3 ligase activity promote transforming growth factor-β-mediated nuclear factor-kB activation during breast cancer progression. J Biol Chem 284: 21209-21217.
    • (2009) J Biol Chem , vol.284 , pp. 21209-21217
    • Neil, J.R.1    Tian, M.2    Schiemann, W.P.3
  • 180
    • 0037085287 scopus 로고    scopus 로고
    • The mode of bone morphogenetic protein (BMP) receptor oligomerization determines different BMP-2 signaling pathways
    • Nohe A, Hassel S, Ehrlich M, Neubauer F, Sebald W, Henis YI, Knaus P. 2002. The mode of bone morphogenetic protein (BMP) receptor oligomerization determines different BMP-2 signaling pathways. J Biol Chem 277: 5330-5338.
    • (2002) J Biol Chem , vol.277 , pp. 5330-5338
    • Nohe, A.1    Hassel, S.2    Ehrlich, M.3    Neubauer, F.4    Sebald, W.5    Henis, Y.I.6    Knaus, P.7
  • 183
    • 14844364701 scopus 로고    scopus 로고
    • Regulation of the polarity protein Par6 by TGFb receptors controls epithelial cell plasticity
    • Ozdamar B, Bose R, Barrios-Rodiles M, Wang HR, Zhang Y, Wrana JL. 2005. Regulation of the polarity protein Par6 by TGFb receptors controls epithelial cell plasticity. Science 307: 1603-1609.
    • (2005) Science , vol.307 , pp. 1603-1609
    • Ozdamar, B.1    Bose, R.2    Barrios-Rodiles, M.3    Wang, H.R.4    Zhang, Y.5    Wrana, J.L.6
  • 186
    • 38349173601 scopus 로고    scopus 로고
    • ALK5- and TGFBR2-independent role of ALK1 in the pathogenesis of hereditary hemorrhagic telangiectasia type 2
    • Park SO, Lee YJ, Seki T, Hong KH, Fliess N, Jiang Z, Park A, Wu X, Kaartinen V, Roman BL, et al. 2008. ALK5- and TGFBR2-independent role of ALK1 in the pathogenesis of hereditary hemorrhagic telangiectasia type 2. Blood 111: 633-642.
    • (2008) Blood , vol.111 , pp. 633-642
    • Park, S.O.1    Lee, Y.J.2    Seki, T.3    Hong, K.H.4    Fliess, N.5    Jiang, Z.6    Park, A.7    Wu, X.8    Kaartinen, V.9    Roman, B.L.10
  • 188
    • 0036272313 scopus 로고    scopus 로고
    • Internalization-dependent and -independent requirements for transforming growth factor b receptor signaling via the Smad pathway
    • Penheiter SG, Mitchell H, Garamszegi N, Edens M, Dore JJ Jr, Leof EB. 2002. Internalization-dependent and -independent requirements for transforming growth factor b receptor signaling via the Smad pathway. Mol Cell Biol 22: 4750-4759.
    • (2002) Mol Cell Biol , vol.22 , pp. 4750-4759
    • Penheiter, S.G.1    Mitchell, H.2    Garamszegi, N.3    Edens, M.4    Dore, J.J.5    Leof, E.B.6
  • 191
    • 0034671578 scopus 로고    scopus 로고
    • TGF-β inhibits p70 S6 kinase via protein phosphatase 2A to induce G1 arrest
    • Petritsch C, Beug H, Balmain A, Oft M. 2000. TGF-β inhibits p70 S6 kinase via protein phosphatase 2A to induce G1 arrest. Genes Dev 14: 3093-3101.
    • (2000) Genes Dev , vol.14 , pp. 3093-3101
    • Petritsch, C.1    Beug, H.2    Balmain, A.3    Oft, M.4
  • 192
    • 84904154934 scopus 로고    scopus 로고
    • Platelet-derived growth factor b-receptor, transforming growth factor b type I receptor, and CD44 protein modulate each other’s signaling and stability
    • Porsch H, Mehic M, Olofsson B, Heldin P, Heldin CH. 2014. Platelet-derived growth factor b-receptor, transforming growth factor b type I receptor, and CD44 protein modulate each other’s signaling and stability. J Biol Chem 289: 19747-19757.
    • (2014) J Biol Chem , vol.289 , pp. 19747-19757
    • Porsch, H.1    Mehic, M.2    Olofsson, B.3    Heldin, P.4    Heldin, C.H.5
  • 193
    • 77649249596 scopus 로고    scopus 로고
    • TGF-β type II receptor phosphorylates PTH receptor to integrate bone remodelling signalling
    • Qiu T, Wu X, Zhang F, Clemens TL, Wan M, Cao X. 2010. TGF-β type II receptor phosphorylates PTH receptor to integrate bone remodelling signalling. Nat Cell Biol 12: 224-234.
    • (2010) Nat Cell Biol , vol.12 , pp. 224-234
    • Qiu, T.1    Wu, X.2    Zhang, F.3    Clemens, T.L.4    Wan, M.5    Cao, X.6
  • 194
    • 77952005098 scopus 로고    scopus 로고
    • Ternary complex of transforming growth factor-β 1 reveals isoform-specific ligand recognition and receptor recruitment in the superfamily
    • Radaev S, Zou ZC, Huang T, Lafer EM, Hinck AP, Sun PD. 2010. Ternary complex of transforming growth factor-β 1 reveals isoform-specific ligand recognition and receptor recruitment in the superfamily. J Biol Chem 285: 14806-14814.
    • (2010) J Biol Chem , vol.285 , pp. 14806-14814
    • Radaev, S.1    Zou, Z.C.2    Huang, T.3    Lafer, E.M.4    Hinck, A.P.5    Sun, P.D.6
  • 195
    • 77950880642 scopus 로고    scopus 로고
    • ALK5 phosphorylation of the endoglin cytoplasmic domain regulates Smad1/5/8 signaling and endothelial cell migration
    • Ray BN, Lee NY, How T, Blobe GC. 2010. ALK5 phosphorylation of the endoglin cytoplasmic domain regulates Smad1/5/8 signaling and endothelial cell migration. Carcinogenesis 31: 435-441.
    • (2010) Carcinogenesis , vol.31 , pp. 435-441
    • Ray, B.N.1    Lee, N.Y.2    How, T.3    Blobe, G.C.4
  • 196
    • 0035794218 scopus 로고    scopus 로고
    • Caveolin-1 regulates transforming growth factor (TGF)-b/SMAD signaling through an interaction with the TGF-β type I receptor
    • Razani B, Zhang XL, Bitzer M, von Gersdorff G, Böttinger EP, Lisanti MP. 2001. Caveolin-1 regulates transforming growth factor (TGF)-b/SMAD signaling through an interaction with the TGF-β type I receptor. J Biol Chem 276: 6727-6738.
    • (2001) J Biol Chem , vol.276 , pp. 6727-6738
    • Razani, B.1    Zhang, X.L.2    Bitzer, M.3    Von Gersdorff, G.4    Böttinger, E.P.5    Lisanti, M.P.6
  • 197
    • 65549084375 scopus 로고    scopus 로고
    • Different domains regulate homomeric and heteromeric complex formation among type I and type II transforming growth factor-b receptors
    • Rechtman MM, Nakaryakov A, Shapira KE, Ehrlich M, Henis YI. 2009. Different domains regulate homomeric and heteromeric complex formation among type I and type II transforming growth factor-b receptors. J Biol Chem 284: 7843-7852.
    • (2009) J Biol Chem , vol.284 , pp. 7843-7852
    • Rechtman, M.M.1    Nakaryakov, A.2    Shapira, K.E.3    Ehrlich, M.4    Henis, Y.I.5
  • 198
    • 84939789948 scopus 로고    scopus 로고
    • Pharmacokinetic, pharmacodynamic and biomarker evaluation of transforming growth factor β receptor I kinase inhibitor, galunisertib, in phase 1 study in patients with advanced cancer
    • Rodon J, Carducci M, Sepulveda-Sanchez JM, Azaro A, Calvo E, Seoane J, Brana I, Sicart E, Gueorguieva I, Cleverly A, et al. 2015a. Pharmacokinetic, pharmacodynamic and biomarker evaluation of transforming growth factor β receptor I kinase inhibitor, galunisertib, in phase 1 study in patients with advanced cancer. Invest New Drugs 33: 357-370.
    • (2015) Invest New Drugs , vol.33 , pp. 357-370
    • Rodon, J.1    Carducci, M.2    Sepulveda-Sanchez, J.M.3    Azaro, A.4    Calvo, E.5    Seoane, J.6    Brana, I.7    Sicart, E.8    Gueorguieva, I.9    Cleverly, A.10
  • 204
    • 33751320113 scopus 로고    scopus 로고
    • Dullard promotes degradation and dephosphorylation of BMP receptors and is required for neural induction
    • Satow R, Kurisaki A, Chan TC, Hamazaki TS, Asashima M. 2006. Dullard promotes degradation and dephosphorylation of BMP receptors and is required for neural induction. Dev Cell 11: 763-774.
    • (2006) Dev Cell , vol.11 , pp. 763-774
    • Satow, R.1    Kurisaki, A.2    Chan, T.C.3    Hamazaki, T.S.4    Asashima, M.5
  • 206
    • 4444249880 scopus 로고    scopus 로고
    • avb3 Integrin interacts with the transforming growth factor b (TGFβ) type II receptor to potentiate the proliferative effects of TGFβ1 in living human lung fibroblasts
    • Scaffidi AK, Petrovic N, Moodley YP, Fogel-Petrovic M, Kroeger KM, Seeber RM, Eidne KA, Thompson PJ, Knight DA. 2004. avb3 Integrin interacts with the transforming growth factor b (TGFβ) type II receptor to potentiate the proliferative effects of TGFβ1 in living human lung fibroblasts. J Biol Chem 279: 37726-37733.
    • (2004) J Biol Chem , vol.279 , pp. 37726-37733
    • Scaffidi, A.K.1    Petrovic, N.2    Moodley, Y.P.3    Fogel-Petrovic, M.4    Kroeger, K.M.5    Seeber, R.M.6    Eidne, K.A.7    Thompson, P.J.8
  • 207
    • 34347230515 scopus 로고    scopus 로고
    • Endoglin differentially modulates antagonistic transforming growth factor-b1 and BMP-7 signaling
    • Scherner O, Meurer SK, Tihaa L, Gressner AM, Weiskirchen R. 2007. Endoglin differentially modulates antagonistic transforming growth factor-b1 and BMP-7 signaling. J Biol Chem 282: 13934-13943.
    • (2007) J Biol Chem , vol.282 , pp. 13934-13943
    • Scherner, O.1    Meurer, S.K.2    Tihaa, L.3    Gressner, A.M.4    Weiskirchen, R.5
  • 208
    • 3142715934 scopus 로고    scopus 로고
    • Transforming growth factor-β (TGF-β)-resistant B cells from chronic lymphocytic leukemia patients contain recurrent mutations in the signal sequence of the type I TGF-β receptor
    • Schiemann WP, Rotzer D, Pfeifer WM, Levi E, Rai KR, Knaus P, Kadin ME. 2004. Transforming growth factor-β (TGF-β)-resistant B cells from chronic lymphocytic leukemia patients contain recurrent mutations in the signal sequence of the type I TGF-β receptor. Cancer Detect Prev 28: 57-64.
    • (2004) Cancer Detect Prev , vol.28 , pp. 57-64
    • Schiemann, W.P.1    Rotzer, D.2    Pfeifer, W.M.3    Levi, E.4    Rai, K.R.5    Knaus, P.6    Kadin, M.E.7
  • 209
  • 210
    • 4544286802 scopus 로고    scopus 로고
    • Molecular recognition in bone morphogenetic protein (BMP)/receptor interaction
    • Sebald W, Nickel J, Zhang JL, Mueller TD. 2004. Molecular recognition in bone morphogenetic protein (BMP)/receptor interaction. Biol Chem 385: 697-710.
    • (2004) Biol Chem , vol.385 , pp. 697-710
    • Sebald, W.1    Nickel, J.2    Zhang, J.L.3    Mueller, T.D.4
  • 211
    • 3042801616 scopus 로고    scopus 로고
    • Transcriptional regulation of the TGF-β pseudoreceptor BAMBI by TGF-β signaling
    • Sekiya T, Oda T, Matsuura K, Akiyama T. 2004. Transcriptional regulation of the TGF-β pseudoreceptor BAMBI by TGF-β signaling. Biochem Biophys Res Commun 320: 680-684.
    • (2004) Biochem Biophys Res Commun , vol.320 , pp. 680-684
    • Sekiya, T.1    Oda, T.2    Matsuura, K.3    Akiyama, T.4
  • 212
    • 84860488299 scopus 로고    scopus 로고
    • miR-192, miR-194, miR-215, miR-200c and miR-141 are downregulated and their common target ACVR2B is strongly expressed in renal childhood neoplasms
    • Senanayake U, Das S, Vesely P, Alzoughbi W, Frohlich LF, Chowdhury P, Leuschner I, Hoefler G, Guertl B. 2012. miR-192, miR-194, miR-215, miR-200c and miR-141 are downregulated and their common target ACVR2B is strongly expressed in renal childhood neoplasms. Carcinogenesis 33: 1014-1021.
    • (2012) Carcinogenesis , vol.33 , pp. 1014-1021
    • Senanayake, U.1    Das, S.2    Vesely, P.3    Alzoughbi, W.4    Frohlich, L.F.5    Chowdhury, P.6    Leuschner, I.7    Hoefler, G.8
  • 213
    • 30044434463 scopus 로고    scopus 로고
    • Regulation of transforming growth factor-b signaling and PDK1 kinase activity by physical interaction between PDK1 and serine-threonine kinase receptor-associated protein
    • Seong HA, Jung H, Choi HS, Kim KT, Ha H. 2005. Regulation of transforming growth factor-b signaling and PDK1 kinase activity by physical interaction between PDK1 and serine-threonine kinase receptor-associated protein. J Biol Chem 280: 42897-42908.
    • (2005) J Biol Chem , vol.280 , pp. 42897-42908
    • Seong, H.A.1    Jung, H.2    Choi, H.S.3    Kim, K.T.4    Ha, H.5
  • 214
    • 34249674439 scopus 로고    scopus 로고
    • NM23-H1 tumor suppressor physically interacts with serine-threonine kinase receptor-associated protein, a transforming growth factor-β (TGF-β) receptor-interacting protein, and negatively regulates TGF-β signaling
    • Seong HA, Jung H, Ha H. 2007. NM23-H1 tumor suppressor physically interacts with serine-threonine kinase receptor-associated protein, a transforming growth factor-β (TGF-β) receptor-interacting protein, and negatively regulates TGF-β signaling. J Biol Chem 282: 12075-12096.
    • (2007) J Biol Chem , vol.282 , pp. 12075-12096
    • Seong, H.A.1    Jung, H.2    Ha, H.3
  • 215
    • 1642539976 scopus 로고    scopus 로고
    • GADD34-PP1c recruited by Smad7 dephosphorylates TGFb type I receptor
    • Shi W, Sun C, He B, Xiong W, Shi X, Yao D, Cao X. 2004. GADD34-PP1c recruited by Smad7 dephosphorylates TGFb type I receptor. J Cell Biol 164: 291-300.
    • (2004) J Cell Biol , vol.164 , pp. 291-300
    • Shi, W.1    Sun, C.2    He, B.3    Xiong, W.4    Shi, X.5    Yao, D.6    Cao, X.7
  • 216
    • 34248231196 scopus 로고    scopus 로고
    • Endofin acts as a Smad anchor for receptor activation in BMP signaling
    • Shi W, Chang C, Nie S, Xie S, Wan M, Cao X. 2007. Endofin acts as a Smad anchor for receptor activation in BMP signaling. J Cell Sci 120: 1216-1224.
    • (2007) J Cell Sci , vol.120 , pp. 1216-1224
    • Shi, W.1    Chang, C.2    Nie, S.3    Xie, S.4    Wan, M.5    Cao, X.6
  • 221
    • 84872790880 scopus 로고    scopus 로고
    • MicroRNA miR-98 inhibits tumor angiogenesis and invasion by targeting activin receptor-like kinase-4 and matrix metalloproteinase-11
    • Siragam V, Rutnam ZJ, Yang WN, Fang L, Luo LL, Yang XL, Li MH, Deng ZQ, Qian J, Peng C, et al. 2012. MicroRNA miR-98 inhibits tumor angiogenesis and invasion by targeting activin receptor-like kinase-4 and matrix metalloproteinase-11. Oncotarget 3: 1370-1385.
    • (2012) Oncotarget , vol.3 , pp. 1370-1385
    • Siragam, V.1    Rutnam, Z.J.2    Yang, W.N.3    Fang, L.4    Luo, L.L.5    Yang, X.L.6    Li, M.H.7    Deng, Z.Q.8    Qian, J.9    Peng, C.10
  • 222
    • 0043164827 scopus 로고    scopus 로고
    • Loss of distinct arterial and venous boundaries in mice lacking endoglin, a vascular-specific TGFb coreceptor
    • Sorensen LK, Brooke BS, Li DY, Urness LD. 2003. Loss of distinct arterial and venous boundaries in mice lacking endoglin, a vascular-specific TGFb coreceptor. Dev Biol 261: 235-250.
    • (2003) Dev Biol , vol.261 , pp. 235-250
    • Sorensen, L.K.1    Brooke, B.S.2    Li, D.Y.3    Urness, L.D.4
  • 224
    • 0029959774 scopus 로고    scopus 로고
    • Phosphorylation of Ser165 in TGF-β type I receptor modulates TGF-β1-induced cellular responses
    • Souchelnytskyi S, ten Dijke P, Miyazono K, Heldin CH. 1996. Phosphorylation of Ser165 in TGF-β type I receptor modulates TGF-β1-induced cellular responses. EMBO J 15: 6231-6240.
    • (1996) EMBO J , vol.15 , pp. 6231-6240
    • Souchelnytskyi, S.1    Ten Dijke, P.2    Miyazono, K.3    Heldin, C.H.4
  • 225
    • 0030613262 scopus 로고    scopus 로고
    • Phosphorylation of Ser465 and Ser467 in the C terminus of Smad2 mediates interaction with Smad4 and is required for transforming growth factor-β signaling
    • Souchelnytskyi S, Tamaki K, Engström U, Wernstedt C, ten Dijke P, Heldin CH. 1997. Phosphorylation of Ser465 and Ser467 in the C terminus of Smad2 mediates interaction with Smad4 and is required for transforming growth factor-β signaling. J Biol Chem 272: 28107-28115.
    • (1997) J Biol Chem , vol.272 , pp. 28107-28115
    • Souchelnytskyi, S.1    Tamaki, K.2    Engström, U.3    Wernstedt, C.4    Ten Dijke, P.5    Heldin, C.H.6
  • 228
    • 33847379496 scopus 로고    scopus 로고
    • The evolutionally conserved activity of Dapper2 in antagonizing TGF-β signaling
    • Su Y, Zhang L, Gao X, Meng F, Wen J, Zhou H, Meng A, Chen YG. 2007. The evolutionally conserved activity of Dapper2 in antagonizing TGF-β signaling. FASEB J 21: 682-690.
    • (2007) FASEB J , vol.21 , pp. 682-690
    • Su, Y.1    Zhang, L.2    Gao, X.3    Meng, F.4    Wen, J.5    Zhou, H.6    Meng, A.7    Chen, Y.G.8
  • 229
    • 79955780736 scopus 로고    scopus 로고
    • Multiple targets of miR-302 and miR-372 promote reprogramming of human fibroblasts to induced pluripotent stem cells
    • Subramanyam D, Lamouille S, Judson RL, Liu JY, Bucay N, Derynck R, Blelloch R. 2011. Multiple targets of miR-302 and miR-372 promote reprogramming of human fibroblasts to induced pluripotent stem cells. Nat Biotechnol 29: 443-448.
    • (2011) Nat Biotechnol , vol.29 , pp. 443-448
    • Subramanyam, D.1    Lamouille, S.2    Judson, R.L.3    Liu, J.Y.4    Bucay, N.5    Derynck, R.6    Blelloch, R.7
  • 230
    • 84892594912 scopus 로고    scopus 로고
    • Role of miR-17 family in the negative feedback loop of bone morphogenetic protein signaling in neuron
    • Sun Q, Mao SS, Li HQ, Zen K, Zhang CY, Li L. 2013. Role of miR-17 family in the negative feedback loop of bone morphogenetic protein signaling in neuron. PLoS ONE 8: e83067.
    • (2013) Plos ONE , vol.8
    • Sun, Q.1    Mao, S.S.2    Li, H.Q.3    Zen, K.4    Zhang, C.Y.5    Li, L.6
  • 231
    • 33947246042 scopus 로고    scopus 로고
    • A novel small-molecule inhibitor of transforming growth factor b type I receptor kinase (SM16) inhibits murine mesothelioma tumor growth in vivo and prevents tumor recurrence after surgical resection
    • Suzuki E, Kim S, Cheung HK, Corbley MJ, Zhang X, Sun L, Shan F, Singh J, Lee WC, Albelda SM, et al. 2007. A novel small-molecule inhibitor of transforming growth factor b type I receptor kinase (SM16) inhibits murine mesothelioma tumor growth in vivo and prevents tumor recurrence after surgical resection. Cancer Res 67: 2351-2359.
    • (2007) Cancer Res , vol.67 , pp. 2351-2359
    • Suzuki, E.1    Kim, S.2    Cheung, H.K.3    Corbley, M.J.4    Zhang, X.5    Sun, L.6    Shan, F.7    Singh, J.8    Lee, W.C.9    Albelda, S.M.10
  • 232
    • 0032531281 scopus 로고    scopus 로고
    • TGF-β receptor expression on human keratinocytes: A 150 kDa GPI-anchored TGF-β1 binding protein forms a heteromeric complex with type I and type II receptors
    • Tam BYY, Germain L, Philip A. 1998. TGF-β receptor expression on human keratinocytes: A 150 kDa GPI-anchored TGF-β1 binding protein forms a heteromeric complex with type I and type II receptors. J Cell Biochem 70: 573-586.
    • (1998) J Cell Biochem , vol.70 , pp. 573-586
    • Tam, B.1    Germain, L.2    Philip, A.3
  • 233
    • 0036911117 scopus 로고    scopus 로고
    • A novel transforming growth factor-b receptor-interacting protein that is also a light chain of the motor protein dynein
    • Tang Q, Staub CM, Gao G, Jin Q, Wang Z, Ding W, Aurigemma RE, Mulder KM. 2002. A novel transforming growth factor-b receptor-interacting protein that is also a light chain of the motor protein dynein. Mol Biol Cell 13: 4484-4496.
    • (2002) Mol Biol Cell , vol.13 , pp. 4484-4496
    • Tang, Q.1    Staub, C.M.2    Gao, G.3    Jin, Q.4    Wang, Z.5    Ding, W.6    Aurigemma, R.E.7    Mulder, K.M.8
  • 235
    • 84943147193 scopus 로고    scopus 로고
    • TbRIII independently binds type I and type II TGF-β receptors to inhibit TGF-β signaling
    • Tazat K, Hector-Greene M, Blobe GC, Henis YI. 2015. TbRIII independently binds type I and type II TGF-β receptors to inhibit TGF-β signaling. Mol Biol Cell 26: 3535-3545.
    • (2015) Mol Biol Cell , vol.26 , pp. 3535-3545
    • Tazat, K.1    Hector-Greene, M.2    Blobe, G.C.3    Henis, Y.I.4
  • 236
    • 35448991324 scopus 로고    scopus 로고
    • Extracellular control of TGFβ signalling in vascular development and disease
    • ten Dijke P, Arthur HM. 2007. Extracellular control of TGFβ signalling in vascular development and disease. Nat Rev Mol Cell Biol 8: 857-869.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 857-869
    • Ten Dijke, P.1    Arthur, H.M.2
  • 237
    • 0346943954 scopus 로고    scopus 로고
    • Familial and sporadic primary pulmonary hypertension is caused by BMPR2 gene mutations resulting in haploinsufficiency of the bone morphogenetic protein type II receptor
    • Thomson J, Machado R, Pauciulo M, Morgan N, Yacoub M, Corris P, McNeil K, Loyd J, Nichols W, Trembath R. 2001. Familial and sporadic primary pulmonary hypertension is caused by BMPR2 gene mutations resulting in haploinsufficiency of the bone morphogenetic protein type II receptor. J Heart Lung Transplant 20: 149.
    • (2001) J Heart Lung Transplant , vol.20
    • Thomson, J.1    Machado, R.2    Pauciulo, M.3    Morgan, N.4    Yacoub, M.5    Corris, P.6    McNeil, K.7    Loyd, J.8    Nichols, W.9    Trembath, R.10
  • 239
    • 0032428684 scopus 로고    scopus 로고
    • SARA, a FYVE domain protein that recruits Smad2 to the TGFb receptor
    • Tsukazaki T, Chiang TA, Davison AF, Attisano L, Wrana JL. 1998. SARA, a FYVE domain protein that recruits Smad2 to the TGFb receptor. Cell 95: 779-791.
    • (1998) Cell , vol.95 , pp. 779-791
    • Tsukazaki, T.1    Chiang, T.A.2    Davison, A.F.3    Attisano, L.4    Wrana, J.L.5
  • 240
    • 7444226411 scopus 로고    scopus 로고
    • SD-208, a novel transforming growth factor b receptor I kinase inhibitor, inhibits growth and invasiveness and enhances immunogenicity of murine and human glioma cells in vitro and in vivo
    • Uhl M, Aulwurm S, Wischhusen J, Weiler M, Ma JY, Almirez R, Mangadu R, Liu YW, Platten M, Herrlinger U, et al. 2004. SD-208, a novel transforming growth factor b receptor I kinase inhibitor, inhibits growth and invasiveness and enhances immunogenicity of murine and human glioma cells in vitro and in vivo. Cancer Res 64: 7954-7961.
    • (2004) Cancer Res , vol.64 , pp. 7954-7961
    • Uhl, M.1    Aulwurm, S.2    Wischhusen, J.3    Weiler, M.4    Ma, J.Y.5    Almirez, R.6    Mangadu, R.7    Liu, Y.W.8    Platten, M.9    Herrlinger, U.10
  • 241
    • 33745188200 scopus 로고    scopus 로고
    • Smad7 and protein phosphatase 1a are critical determinants in the duration of TGFb/ALK1 signaling in endothelial cells
    • Valdimarsdóttir G, Goumans MJ, Itoh F, Itoh S, Heldin CH, ten Dijke P. 2006. Smad7 and protein phosphatase 1a are critical determinants in the duration of TGFb/ALK1 signaling in endothelial cells. BMC Cell Biol 7: 16.
    • (2006) BMC Cell Biol , vol.7
    • Valdimarsdóttir, G.1    Goumans, M.J.2    Itoh, F.3    Itoh, S.4    Heldin, C.H.5    Ten Dijke, P.6
  • 242
    • 77953497987 scopus 로고    scopus 로고
    • ALK2 R206H mutation linked to fibrodysplasia ossificans progressiva confers constitutive activity to the BMP type I receptor and sensitizes mesenchymal cells to BMP-induced osteoblast differentiation and bone formation
    • van Dinther M, Visser N, de Gorter DJJ, Doorn J, Goumans MJ, de Boer J, ten Dijke P. 2010. ALK2 R206H mutation linked to fibrodysplasia ossificans progressiva confers constitutive activity to the BMP type I receptor and sensitizes mesenchymal cells to BMP-induced osteoblast differentiation and bone formation. J Bone Miner Res 25: 1208-1215.
    • (2010) J Bone Miner Res , vol.25 , pp. 1208-1215
    • Van Dinther, M.1    Visser, N.2    De Gorter, D.3    Doorn, J.4    Goumans, M.J.5    De Boer, J.6    Ten Dijke, P.7
  • 243
    • 84861557944 scopus 로고    scopus 로고
    • Anti-human activin receptor-like kinase 1 (ALK1) antibody attenuates bone morphogenetic protein 9 (BMP9)-induced ALK1 signaling and interferes with endothelial cell sprouting
    • van Meeteren LA, Thorikay M, Bergqvist S, Pardali E, Gallo Stampino C, Hu-Lowe D, Goumans MJ, Ten Dijke P. 2012. Anti-human activin receptor-like kinase 1 (ALK1) antibody attenuates bone morphogenetic protein 9 (BMP9)-induced ALK1 signaling and interferes with endothelial cell sprouting. J Biol Chem 287: 18551-18561.
    • (2012) J Biol Chem , vol.287 , pp. 18551-18561
    • Van Meeteren, L.A.1    Thorikay, M.2    Bergqvist, S.3    Pardali, E.4    Gallo Stampino, C.5    Hu-Lowe, D.6    Goumans, M.J.7    Ten Dijke, P.8
  • 245
    • 84876817355 scopus 로고    scopus 로고
    • Beyond TGFb: Roles of other TGFb superfamily members in cancer
    • Wakefield LM, Hill CS. 2013. Beyond TGFb: Roles of other TGFb superfamily members in cancer. Nat Rev Cancer 13: 328-341.
    • (2013) Nat Rev Cancer , vol.13 , pp. 328-341
    • Wakefield, L.M.1    Hill, C.S.2
  • 247
    • 38349146518 scopus 로고    scopus 로고
    • MicroRNA miR-24 inhibits erythropoiesis by targeting activin type I receptor ALK4
    • Wang Q, Huang Z, Xue H, Jin C, Ju XL, Han JD, Chen Y-G. 2008. MicroRNA miR-24 inhibits erythropoiesis by targeting activin type I receptor ALK4. Blood 111: 588-595.
    • (2008) Blood , vol.111 , pp. 588-595
    • Wang, Q.1    Huang, Z.2    Xue, H.3    Jin, C.4    Ju, X.L.5    Han, J.D.6    Chen, Y.-G.7
  • 248
    • 84895900338 scopus 로고    scopus 로고
    • Transforming growth factor-b 1-mediated renal fibrosis is dependent on the regulation of transforming growth factor receptor 1 expression by let-7b
    • Wang B, Jha JC, Hagiwara S, McClelland AD, Jandeleit-Dahm K, Thomas MC, Cooper ME, Kantharidis P. 2014. Transforming growth factor-b 1-mediated renal fibrosis is dependent on the regulation of transforming growth factor receptor 1 expression by let-7b. Kidney Int 85: 352-361.
    • (2014) Kidney Int , vol.85 , pp. 352-361
    • Wang, B.1    Jha, J.C.2    Hagiwara, S.3    McClelland, A.D.4    Jandeleit-Dahm, K.5    Thomas, M.C.6    Cooper, M.E.7    Kantharidis, P.8
  • 249
    • 0030030373 scopus 로고    scopus 로고
    • Complementation between kinase-defective and activation-defective TGF-β receptors reveals a novel form of receptor cooperativity essential for signaling
    • Weis-Garcia F, Massagué J. 1996. Complementation between kinase-defective and activation-defective TGF-β receptors reveals a novel form of receptor cooperativity essential for signaling. EMBO J 15: 276-289.
    • (1996) EMBO J , vol.15 , pp. 276-289
    • Weis-Garcia, F.1    Massagué, J.2
  • 250
    • 0033605117 scopus 로고    scopus 로고
    • Transforming growth factor-b induces formation of a dithiothreitol-resistant type I/type II receptor complex in live cells
    • Wells RG, Gilboa L, Sun Y, Liu XD, Henis YI, Lodish HF. 1999. Transforming growth factor-b induces formation of a dithiothreitol-resistant type I/type II receptor complex in live cells. J Biol Chem 274: 5716-5722.
    • (1999) J Biol Chem , vol.274 , pp. 5716-5722
    • Wells, R.G.1    Gilboa, L.2    Sun, Y.3    Liu, X.D.4    Henis, Y.I.5    Lodish, H.F.6
  • 251
    • 33745195026 scopus 로고    scopus 로고
    • Identification of distinct inhibin and transforming growth factor β-binding sites on betaglycan: Functional separation of betaglycan co-receptor actions
    • Wiater E, Harrison CA, Lewis KA, Gray PC, Vale WW. 2006. Identification of distinct inhibin and transforming growth factor β-binding sites on betaglycan: Functional separation of betaglycan co-receptor actions. J Biol Chem 281: 17011-17022.
    • (2006) J Biol Chem , vol.281 , pp. 17011-17022
    • Wiater, E.1    Harrison, C.A.2    Lewis, K.A.3    Gray, P.C.4    Vale, W.W.5
  • 252
    • 27644572195 scopus 로고    scopus 로고
    • Bone morphogenetic protein receptor type II C-terminus interacts with c-Src: Implication for a role in pulmonary arterial hypertension
    • Wong WK, Knowles JA, Morse JH. 2005. Bone morphogenetic protein receptor type II C-terminus interacts with c-Src: Implication for a role in pulmonary arterial hypertension. Am J Respir Cell Mol Biol 33: 438-446.
    • (2005) Am J Respir Cell Mol Biol , vol.33 , pp. 438-446
    • Wong, W.K.1    Knowles, J.A.2    Morse, J.H.3
  • 254
    • 48249099342 scopus 로고    scopus 로고
    • Critical regulation of TGFb signaling by Hsp90
    • Wrighton KH, Lin X, Feng X-H. 2008. Critical regulation of TGFb signaling by Hsp90. Proc Natl Acad Sci 105: 9244-9249.
    • (2008) Proc Natl Acad Sci , vol.105 , pp. 9244-9249
    • Wrighton, K.H.1    Lin, X.2    Feng, X.-H.3
  • 255
    • 58149239730 scopus 로고    scopus 로고
    • Phospho-control of TGF-β superfamily signaling
    • Wrighton KH, Lin X, Feng XH. 2009a. Phospho-control of TGF-β superfamily signaling. Cell Res 19: 8-20.
    • (2009) Cell Res , vol.19 , pp. 8-20
    • Wrighton, K.H.1    Lin, X.2    Feng, X.H.3
  • 256
    • 65649105437 scopus 로고    scopus 로고
    • Transforming growth factor b can stimulate Smad1 phosphorylation independently of bone morphogenic protein receptors
    • Wrighton KH, Lin X, Yu PB, Feng XH. 2009b. Transforming growth factor b can stimulate Smad1 phosphorylation independently of bone morphogenic protein receptors. J Biol Chem 284: 9755-9763.
    • (2009) J Biol Chem , vol.284 , pp. 9755-9763
    • Wrighton, K.H.1    Lin, X.2    Yu, P.B.3    Feng, X.H.4
  • 257
    • 67650225263 scopus 로고    scopus 로고
    • Essential role of TGF-β signaling in glucose-induced cell hypertrophy
    • Wu LY, Derynck R. 2009. Essential role of TGF-β signaling in glucose-induced cell hypertrophy. Dev Cell 17: 35-48.
    • (2009) Dev Cell , vol.17 , pp. 35-48
    • Wu, L.Y.1    Derynck, R.2
  • 259
    • 38149019302 scopus 로고    scopus 로고
    • Genomewide impact of the BRG1 SWI/SNF chromatin remodeler on the transforming growth factor b transcriptional program
    • Xi Q, He W, Zhang XH, Le HV, Massague J. 2008. Genomewide impact of the BRG1 SWI/SNF chromatin remodeler on the transforming growth factor b transcriptional program. J Biol Chem 283: 1146-1155.
    • (2008) J Biol Chem , vol.283 , pp. 1146-1155
    • Xi, Q.1    He, W.2    Zhang, X.H.3    Le, H.V.4    Massague, J.5
  • 260
    • 34547124340 scopus 로고    scopus 로고
    • Repulsive guidance molecule RGMa alters utilization of bone morphogenetic protein (BMP) type II receptors by BMP2 and BMP4
    • Xia Y, Yu PB, Sidis Y, Beppu H, Bloch KD, Schneyer AL, Lin HY. 2007. Repulsive guidance molecule RGMa alters utilization of bone morphogenetic protein (BMP) type II receptors by BMP2 and BMP4. J Biol Chem 282: 18129-18140.
    • (2007) J Biol Chem , vol.282 , pp. 18129-18140
    • Xia, Y.1    Yu, P.B.2    Sidis, Y.3    Beppu, H.4    Bloch, K.D.5    Schneyer, A.L.6    Lin, H.Y.7
  • 262
    • 84957659710 scopus 로고    scopus 로고
    • CIN85 modulates TGFb signaling by promoting the presentation of TGFb receptors on the cell surface
    • Yakymovych I, Yakymovych M, Zang G, Mu Y, Bergh A, Landström M, Heldin CH. 2015. CIN85 modulates TGFb signaling by promoting the presentation of TGFb receptors on the cell surface. J Cell Biol 210: 319-332.
    • (2015) J Cell Biol , vol.210 , pp. 319-332
    • Yakymovych, I.1    Yakymovych, M.2    Zang, G.3    Mu, Y.4    Bergh, A.5    Landström, M.6    Heldin, C.H.7
  • 263
    • 0027930903 scopus 로고
    • Formation of hetero-oligomeric complexes of type I and type II receptors for transforming growth factor-β
    • Yamashita H, ten Dijke P, Franzén P, Miyazono K, Heldin CH. 1994. Formation of hetero-oligomeric complexes of type I and type II receptors for transforming growth factor-β. J Biol Chem 269: 20172-20178.
    • (1994) J Biol Chem , vol.269 , pp. 20172-20178
    • Yamashita, H.1    Ten Dijke, P.2    Franzén, P.3    Miyazono, K.4    Heldin, C.H.5
  • 264
    • 52049111663 scopus 로고    scopus 로고
    • TRAF6 mediates Smad-independent activation of JNK and p38 by TGF-β
    • Yamashita M, Fatyol K, Jin C, Wang X, Liu Z, Zhang YE. 2008. TRAF6 mediates Smad-independent activation of JNK and p38 by TGF-β. Mol Cell 31: 918-924.
    • (2008) Mol Cell , vol.31 , pp. 918-924
    • Yamashita, M.1    Fatyol, K.2    Jin, C.3    Wang, X.4    Liu, Z.5    Zhang, Y.E.6
  • 266
    • 71049139747 scopus 로고    scopus 로고
    • Human BAMBI cooperates with Smad7 to inhibit transforming growth factor-b signaling
    • Yan X, Lin Z, Chen F, Zhao X, Chen H, Ning Y, Chen YG. 2009. Human BAMBI cooperates with Smad7 to inhibit transforming growth factor-b signaling. J Biol Chem 284: 30097-30104.
    • (2009) J Biol Chem , vol.284 , pp. 30097-30104
    • Yan, X.1    Lin, Z.2    Chen, F.3    Zhao, X.4    Chen, H.5    Ning, Y.6    Chen, Y.G.7
  • 267
    • 80052572648 scopus 로고    scopus 로고
    • TSC-22 promotes transforming growth factor b-mediated cardiac myofibroblast differentiation by antagonizing Smad7 activity
    • Yan X, Zhang J, Pan L, Wang P, Xue H, Zhang L, Gao X, Zhao X, Ning Y, Chen YG. 2011. TSC-22 promotes transforming growth factor b-mediated cardiac myofibroblast differentiation by antagonizing Smad7 activity. Mol Cell Biol 31: 3700-3709.
    • (2011) Mol Cell Biol , vol.31 , pp. 3700-3709
    • Yan, X.1    Zhang, J.2    Pan, L.3    Wang, P.4    Xue, H.5    Zhang, L.6    Gao, X.7    Zhao, X.8    Ning, Y.9    Chen, Y.G.10
  • 268
    • 84866627838 scopus 로고    scopus 로고
    • MicroRNA-145 suppresses mouse granulosa cell proliferation by targeting activin receptor IB
    • Yan GJ, Zhang LX, Fang T, Zhang Q, Wu SG, Jiang Y, Sun HX, Hu YL. 2012. MicroRNA-145 suppresses mouse granulosa cell proliferation by targeting activin receptor IB. FEBS Lett 586: 3263-3270.
    • (2012) FEBS Lett , vol.586 , pp. 3263-3270
    • Yan, G.J.1    Zhang, L.X.2    Fang, T.3    Zhang, Q.4    Wu, S.G.5    Jiang, Y.6    Sun, H.X.7    Hu, Y.L.8
  • 269
    • 84879607251 scopus 로고    scopus 로고
    • MicroRNA-140-5p suppresses tumor growth and metastasis by targeting transforming growth factor b receptor 1 and fibroblast growth factor 9 in hepatocellular carcinoma
    • Yang H, Fang F, Chang RM, Yang LY. 2013. MicroRNA-140-5p suppresses tumor growth and metastasis by targeting transforming growth factor b receptor 1 and fibroblast growth factor 9 in hepatocellular carcinoma. Hepatology 58: 205-217.
    • (2013) Hepatology , vol.58 , pp. 205-217
    • Yang, H.1    Fang, F.2    Chang, R.M.3    Yang, L.Y.4
  • 270
    • 1842832338 scopus 로고    scopus 로고
    • Transforming growth factor-b receptors interact with AP2 by direct binding to b2 subunit
    • Yao DY, Ehrlich M, Henis YI, Leof EB. 2002. Transforming growth factor-b receptors interact with AP2 by direct binding to b2 subunit. Mol Biol Cell 13: 4001-4012.
    • (2002) Mol Biol Cell , vol.13 , pp. 4001-4012
    • Yao, D.Y.1    Ehrlich, M.2    Henis, Y.I.3    Leof, E.B.4
  • 271
    • 79551553893 scopus 로고    scopus 로고
    • MicroRNA 376c enhances ovarian cancer cell survival by targeting activin receptor-like kinase 7: Implications for chemoresistance
    • Ye G, Fu GD, Cui SY, Zhao SF, Bernaudo S, Bai Y, Ding YF, Zhang YO, Yang BB, Peng C. 2011. MicroRNA 376c enhances ovarian cancer cell survival by targeting activin receptor-like kinase 7: Implications for chemoresistance. J Cell Sci 124: 359-368.
    • (2011) J Cell Sci , vol.124 , pp. 359-368
    • Ye, G.1    Fu, G.D.2    Cui, S.Y.3    Zhao, S.F.4    Bernaudo, S.5    Bai, Y.6    Ding, Y.F.7    Zhang, Y.O.8    Yang, B.B.9    Peng, C.10
  • 272
    • 15444372825 scopus 로고    scopus 로고
    • Type I transforming growth factor b receptor binds to and activates phosphatidylinositol 3-kinase
    • Yi JY, Shin I, Arteaga CL. 2005. Type I transforming growth factor b receptor binds to and activates phosphatidylinositol 3-kinase. J Biol Chem 280: 10870-10876.
    • (2005) J Biol Chem , vol.280 , pp. 10870-10876
    • Yi, J.Y.1    Shin, I.2    Arteaga, C.L.3
  • 273
    • 84880426693 scopus 로고    scopus 로고
    • Retromer maintains basolateral distribution of the type II TGF-β receptor via the recycling endosome
    • Yin XQ, Murphy SJ, Wilkes MC, Ji Y, Leof EB. 2013. Retromer maintains basolateral distribution of the type II TGF-β receptor via the recycling endosome. Mol Biol Cell 24: 2285-2298.
    • (2013) Mol Biol Cell , vol.24 , pp. 2285-2298
    • Yin, X.Q.1    Murphy, S.J.2    Wilkes, M.C.3    Ji, Y.4    Leof, E.B.5
  • 274
    • 10444261212 scopus 로고    scopus 로고
    • Development of TGF-β signalling inhibitors for cancer therapy
    • Yingling JM, Blanchard KL, Sawyer JS. 2004. Development of TGF-β signalling inhibitors for cancer therapy. Nat Rev Drug Discov 3: 1011-1022.
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 1011-1022
    • Yingling, J.M.1    Blanchard, K.L.2    Sawyer, J.S.3
  • 275
    • 36949015426 scopus 로고    scopus 로고
    • The type III TGF-β receptor signals through both Smad3 and the p38 MAP kinase pathways to contribute to inhibition of cell proliferation
    • You HJ, Bruinsma MW, How T, Ostrander JH, Blobe GC. 2007. The type III TGF-β receptor signals through both Smad3 and the p38 MAP kinase pathways to contribute to inhibition of cell proliferation. Carcinogenesis 28: 2491-2500.
    • (2007) Carcinogenesis , vol.28 , pp. 2491-2500
    • You, H.J.1    Bruinsma, M.W.2    How, T.3    Ostrander, J.H.4    Blobe, G.C.5
  • 276
    • 84877705727 scopus 로고    scopus 로고
    • TGF-β-activated kinase 1 (Tak1) mediates agonist-induced Smad activation and linker region phosphorylation in embryonic craniofacial neural crest-derived cells
    • Yumoto K, Thomas PS, Lane J, Matsuzaki K, Inagaki M, Ninomiya-Tsuji J, Scott GJ, Ray MK, Ishii M, Maxson R, et al. 2013. TGF-β-activated kinase 1 (Tak1) mediates agonist-induced Smad activation and linker region phosphorylation in embryonic craniofacial neural crest-derived cells. J Biol Chem 288: 13467-13480.
    • (2013) J Biol Chem , vol.288 , pp. 13467-13480
    • Yumoto, K.1    Thomas, P.S.2    Lane, J.3    Matsuzaki, K.4    Inagaki, M.5    Ninomiya-Tsuji, J.6    Scott, G.J.7    Ray, M.K.8    Ishii, M.9    Maxson, R.10
  • 277
    • 84864286762 scopus 로고    scopus 로고
    • MicroRNA-100 regulates osteogenic differentiation of human adipose-derived mesenchymal stem cells by targeting BMPR2
    • Zeng Y, Qu XB, Li HL, Huang S, Wang SH, Xu QL, Lin RZ, Han Q, Li J, Zhao RC. 2012. MicroRNA-100 regulates osteogenic differentiation of human adipose-derived mesenchymal stem cells by targeting BMPR2. FEBS Lett 586: 2375-2381.
    • (2012) FEBS Lett , vol.586 , pp. 2375-2381
    • Zeng, Y.1    Qu, X.B.2    Li, H.L.3    Huang, S.4    Wang, S.H.5    Xu, Q.L.6    Lin, R.Z.7    Han, Q.8    Li, J.9    Zhao, R.C.10
  • 278
    • 70349443042 scopus 로고    scopus 로고
    • Single-molecule imaging reveals transforming growth factor-b-induced type II receptor dimerization
    • Zhang W, Jiang Y, Wang Q, Ma X, Xiao Z, Zuo W, Fang X, Chen YG. 2009a. Single-molecule imaging reveals transforming growth factor-b-induced type II receptor dimerization. Proc Natl Acad Sci 106: 15679-15683.
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 15679-15683
    • Zhang, W.1    Jiang, Y.2    Wang, Q.3    Ma, X.4    Xiao, Z.5    Zuo, W.6    Fang, X.7    Chen, Y.G.8
  • 279
    • 69449094525 scopus 로고    scopus 로고
    • Rock2 controls TGFb signaling and inhibits mesoderm induction in zebrafish embryos
    • Zhang Y, Li X, Qi J, Wang J, Liu X, Zhang H, Lin SC, Meng A. 2009b. Rock2 controls TGFb signaling and inhibits mesoderm induction in zebrafish embryos. J Cell Sci 122: 2197-2207.
    • (2009) J Cell Sci , vol.122 , pp. 2197-2207
    • Zhang, Y.1    Li, X.2    Qi, J.3    Wang, J.4    Liu, X.5    Zhang, H.6    Lin, S.C.7    Meng, A.8
  • 280
  • 283
    • 84875170985 scopus 로고    scopus 로고
    • MicroRNA-181a suppresses mouse granulosa cell proliferation by targeting activin receptor IIA
    • Zhang Q, Sun HX, Jiang Y, Ding LJ, Wu SG, Fang T, Yan GJ, Hu YL. 2013b. MicroRNA-181a suppresses mouse granulosa cell proliferation by targeting activin receptor IIA. PLoS ONE 8: 59667.
    • (2013) Plos ONE , vol.8
    • Zhang, Q.1    Sun, H.X.2    Jiang, Y.3    Ding, L.J.4    Wu, S.G.5    Fang, T.6    Yan, G.J.7    Hu, Y.L.8
  • 284
    • 76749102053 scopus 로고    scopus 로고
    • Anti-transforming growth factor b receptor II antibody has therapeutic efficacy against primary tumor growth and metastasis through multieffects on cancer, stroma, and immune cells
    • Zhong ZJ, Carroll KD, Policarpio D, Osborn C, Gregory M, Bassi R, Jimenez X, Prewett M, Liebisch G, Persaud K, et al. 2010. Anti-transforming growth factor b receptor II antibody has therapeutic efficacy against primary tumor growth and metastasis through multieffects on cancer, stroma, and immune cells. Clin Cancer Res 16: 1191-1205.
    • (2010) Clin Cancer Res , vol.16 , pp. 1191-1205
    • Zhong, Z.J.1    Carroll, K.D.2    Policarpio, D.3    Osborn, C.4    Gregory, M.5    Bassi, R.6    Jimenez, X.7    Prewett, M.8    Liebisch, G.9    Persaud, K.10
  • 285
    • 84876182757 scopus 로고    scopus 로고
    • BMP receptor-integrin interaction mediates responses of vascular endothelial Smad1/5 and proliferation to disturbed flow
    • Zhou J, Lee PL, Lee CI, Wei SY, Lim SH, Lin TE, Chien S, Chiu JJ. 2013. BMP receptor-integrin interaction mediates responses of vascular endothelial Smad1/5 and proliferation to disturbed flow. J Thromb Haemost 11: 741-755.
    • (2013) J Thromb Haemost , vol.11 , pp. 741-755
    • Zhou, J.1    Lee, P.L.2    Lee, C.I.3    Wei, S.Y.4    Lim, S.H.5    Lin, T.E.6    Chien, S.7    Chiu, J.J.8
  • 286
    • 84906545323 scopus 로고    scopus 로고
    • Micro-RNA-130a is up-regulated in mouse liver by iron deficiency and targets the bone morphogenetic protein (BMP) receptor ALK2 to attenuate BMP signaling and hepcidin transcription
    • Zumbrennen-Bullough KB, Wu QF, Core AB, Canali S, Chen WJ, Theurl I, Meynard D, Babitt JL. 2014. Micro-RNA-130a is up-regulated in mouse liver by iron deficiency and targets the bone morphogenetic protein (BMP) receptor ALK2 to attenuate BMP signaling and hepcidin transcription. J Biol Chem 289: 23796-23808.
    • (2014) J Biol Chem , vol.289 , pp. 23796-23808
    • Zumbrennen-Bullough, K.B.1    Wu, Q.F.2    Core, A.B.3    Canali, S.4    Chen, W.J.5    Theurl, I.6    Meynard, D.7    Babitt, J.L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.